Protein Information

Name catalase
Synonyms CAT; Catalase; Erythrocyte derived growth promoting factor; Carnitine O acetyltransferase; Carnitine acetylase; Carnitine acetyltransferase; CAT; Catalases…

Compound Information

Name sodium azide
CAS sodium azide

Reference List

PubMed Abstract RScore(About this table)
8033320 Li Y, Trush MA, Yager JD: DNA damage caused by reactive oxygen species originating from a copper-dependent oxidation of the 2-hydroxy catechol of estradiol. Plant Cell. 1997 Feb;9(2):209-21.

The appearance of strand breaks was also blocked by catalase and inhibited by the singlet oxygen scavengers sodium azide and 2,2,6,6-tetramethyl-4-piperidone.
81(1,1,1,1) Details
7964128 van der Vliet A, Hu ML, O'Neill CA, Cross CE, Halliwell B: Interactions of human blood plasma with hydrogen peroxide and hypochlorous acid. J Lab Clin Med. 1994 Nov;124(5):701-7.

Hydrogen peroxide at concentrations below 0.5 mmol/L had little effect, but 1 to 2 mmol/L H2O2 caused loss of ascorbic acid and protein thiol groups, an effect potentiated by preincubation of the plasma with sodium azide to inhibit catalase.
81(1,1,1,1) Details
15694276 Sanchis-Segura C, Correa M, Miquel M, Aragon CM: Catalase inhibition in the Arcuate nucleus blocks ethanol effects on the locomotor activity of rats. J Med Microbiol. 1996 Nov;45(5):383-7.

In the present study we have assessed the effect in rats of intraperitoneal, intraventricular or intracraneal administration of the catalase inhibitor sodium azide in the locomotor changes observed after ethanol (1 g/kg) administration.
40(0,1,2,5) Details
8719811 Mian KB, Martin W: The inhibitory effect of 3-amino-1,2,4-triazole on relaxation induced by hydroxylamine and sodium azide but not hydrogen peroxide or glyceryl trinitrate in rat aorta. J Immunol Methods. 1997 Dec 15;210(1):1-10.

These data suggest that metabolism by catalase plays an important role in the relaxation induced by hydroxylamine and sodium azide in isolated rings of rat aorta.
39(0,1,2,4) Details
7625566 Reddy BV, Boyadjieva N, Sarkar DK: Effect of ethanol, propanol, butanol, and catalase enzyme blockers on beta-endorphin secretion from primary cultures of hypothalamic neurons: evidence for a mediatory role of acetaldehyde in ethanol stimulation of beta-endorphin release. Bull Acad Natl Med. 1996 Mar;180(3):697-706; discussion 706-8.

Another catalase inhibitor, sodium azide (5 mM), also inhibited ethanol-stimulated IR-beta-EP secretion.
34(0,1,1,4) Details
16123765 Arizzi-LaFrance MN, Correa M, Aragon CM, Salamone JD: Motor stimulant effects of ethanol injected into the substantia nigra pars reticulata: importance of catalase-mediated metabolism and the role of acetaldehyde. Environ Res. 1994 Aug;66(2):208-16.

The locomotor effects of intranigral ethanol (1.4 micromol) were reduced by coadministration of 10 mg/kg sodium azide, a catalase inhibitor that acts to reduce the metabolism of ethanol into acetaldehyde in the brain.
33(0,1,1,3) Details
11596115 Del Bufalo D, Trisciuoglio D, Biroccio A, Marcocci L, Buglioni S, Candiloro A, Scarsella M, Leonetti C, Zupi G: Bcl-2 overexpression decreases BCNU sensitivity of a human glioblastoma line through enhancement of catalase activity. J Lab Clin Med. 1998 Oct;132(4):294-302.

The ability of the catalase inhibitor, sodium azide, to increase the BCNU sensitivity of the bcl-2 transfectants to levels of the BCNU-treated control clone substantiated the role of the catalase activity.
33(0,1,1,3) Details
17980789 Nizhnikov ME, Molina JC, Spear NE: Central reinforcing effects of ethanol are blocked by catalase inhibition. . Carcinogenesis. 1994 Jul;15(7):1421-7.

Half of the animals corresponding to each learning condition were pretreated with IC administrations of either physiological saline or a catalase inhibitor (sodium-azide).
37(0,1,1,7) Details
16930212 Zimatkin SM, Pronko SP, Vasiliou V, Gonzalez FJ, Deitrich RA: Enzymatic mechanisms of ethanol oxidation in the brain. . Bioorg Khim. 2003 Nov-Dec;29(6):632-9.

RESULTS: The catalase inhibitors sodium azide (5 mM) and aminotriazole (5 mM) as well as CYP2E1 inhibitors diallyl sulfide (2 mM) and beta-phenethyl isothiocyanate (0.1 mM) lowered significantly the accumulation of the ethanol-derived AC and acetate in brain homogenates.
36(0,1,1,6) Details
9726283 Tillonen J, Kaihovaara P, Jousimies-Somer H, Heine R, Salaspuro M: Role of catalase in in vitro acetaldehyde formation by human colonic contents. Biol Pharm Bull. 1997 Aug;20(8):910-2.

The catalase inhibitors sodium azide and 3-amino-1,2,4-triazole (3-AT) markedly reduced the amount of acetaldehyde produced from 22 mM ethanol in a concentration dependent manner compared with the control samples (0.1 mM sodium azide to 73% and 10 mM 3-AT to 67% of control).
36(0,1,1,6) Details
18587667 Correa M, Manrique HM, Font L, Escrig MA, Aragon CM: Reduction in the anxiolytic effects of ethanol by centrally formed acetaldehyde: the role of catalase inhibitors and acetaldehyde-sequestering agents. Biochemistry. 1993 Aug 31;32(34):8955-62.

MATERIALS AND METHODS: The effects of the catalase inhibitor sodium azide (SA; 0 or 10 mg/kg, IP) on ethanol-induced anxiolysis (0.0, 0.5, or 1.0 g/kg, IP) were evaluated in CD1 mice in two anxiety paradigms, the elevated plus maze and the dark/light box.
35(0,1,1,5) Details
16102377 Manrique HM, Miquel M, Aragon CM: Brain catalase mediates potentiation of social recognition memory produced by ethanol in mice. Toxicol Mech Methods. 2009 Feb;19(2):86-93.

Additionally, adult mice received aminotriazole (AT) or sodium azide (two catalase inhibitors) 5h or 30 min before juvenile presentation, respectively.
34(0,1,1,4) Details
17597213 Jamal M, Ameno K, Uekita I, Kumihashi M, Wang W, Ijiri I: Catalase mediates acetaldehyde formation in the striatum of free-moving rats. Ukr Biokhim Zh. 2005 Jul-Aug;77(4):120-3.

Rats received intraperitoneal EtOH (1g/kg) alone or in combination with 4-methylpyrazole (MP, 82 mg/kg, an alcohol dehydrogenase inhibitor), and/or catalase inhibitor sodium azide (AZ, 10mg/kg) or 3-amino-1,2,4-triazole (AT, 1g/kg), and/or cyanamide (CY, 50mg/kg, an aldehyde dehydrogenase inhibitor).
34(0,1,1,4) Details
11834210 Tedesco I, Luigi Russo G, Nazzaro F, Russo M, Palumbo R: Antioxidant effect of red wine anthocyanins in normal and catalase-inactive human erythrocytes. Alcohol. 1999 Aug;19(1):37-42.

Subsequently, we demonstrate that fractions containing anthocyanins lower ROS (reactive oxygen species) and methemoglobin production in human erythrocytes treated with H (2) O (2.) Finally, we reported that the protective effects of anthocyanins were also confirmed in an experimental model in which RBCs were deprived of catalase activity by treatment with 4 mM sodium azide.
32(0,1,1,2) Details
15258675 Kartvelishvili T, Abuladze M, Asatiani N, Akhvlediani J, Asanishvili L, Holman HY, Sapojnikova N: Antioxidant capacity of cultured mammalian cells estimated by ESR method. J Bacteriol. 2002 Jun;184(12):3305-12.

The effects of catalase inhibitors, such as sodium azide and 3-amino-1,2,4-triazole, on the antioxidant capacity of cells were tested.
32(0,1,1,2) Details
11811525 Ogino K, Kodama N, Nakajima M, Yamada A, Nakamura H, Nagase H, Sadamitsu D, Maekawa T: Catalase catalyzes nitrotyrosine formation from sodium azide and hydrogen peroxide. Drug Alcohol Depend. 2005 Sep 1;79(3):343-50. Epub 2005 Apr 22.
166(2,2,2,6) Details
7861697 Li JZ, Sharma R, Dileepan KN, Savin VJ: Polymorphonuclear leukocytes increase glomerular albumin permeability via hypohalous acid. Prostate. 1997 Aug 1;32(3):188-95.

This increase in Palbumin was inhibited by superoxide dismutase, catalase, or taurine (Palbumin = 0.035 +/- 0.06, -0.39 +/- 0.10, 0.028 +/- 0.06, respectively) and ameliorated by sodium azide (Palbumin = 0.21 +/- 0.03).
31(0,1,1,1) Details
7663419 Mao Y, Zang L, Shi X: Singlet oxygen generation in the superoxide reaction. Alcohol Clin Exp Res. 2001 Feb;25(2):253-60.

Catalase and sodium azide inhibited 1O2 generation and H2O2 enhanced it.
31(0,1,1,1) Details
10487386 Sanchis-Segura C, Miquel M, Correa M, Aragon CM: The catalase inhibitor sodium azide reduces ethanol-induced locomotor activity. Photochem Photobiol. 1994 Mar;59(3):343-9.

Moreover, perfused brain homogenates of mice treated with sodium azide also showed a significant reduction of catalase activity.
152(1,3,4,7) Details
7931250 Barwell CJ, Ebrahimi SA: Some problems associated with measuring monoamine oxidase activity in the presence of sodium azide. Biochim Biophys Acta. 1997 May 22;1326(1):124-30.

The colourimetric assay of monoamine oxidase activity, as hydrogen peroxide production, normally requires the use of sodium azide to inhibit breakdown of hydrogen peroxide by catalase.
113(1,2,2,3) Details
12851742 Guitton J, Servanin S, Francina A: Hexose monophosphate shunt activities in human erythrocytes during oxidative damage induced by hydrogen peroxide. Arch Toxicol. 2003 Jul;77(7):410-7. Epub 2003 Mar 14.

Inhibition of catalase by 3-amino-1,2,4-triazole (3-AT) or by sodium azide, followed by a bolus of H (2) O (2) led to a two- to five-fold increases in (13) CO (2) production compared with controls, depending on H (2) O (2) concentration.
32(0,1,1,2) Details
15644086 Lucchi L, Bergamini S, Iannone A, Perrone S, Stipo L, Olmeda F, Caruso F, Tomasi A, Albertazzi A: Erythrocyte susceptibility to oxidative stress in chronic renal failure patients under different substitutive treatments. Artif Organs. 2005 Jan;29(1):67-72.

Their RBCs were incubated with the oxidative stress-inducing agent tert-butylhydroperoxide both in the presence and in the absence of the catalase inhibitor sodium azide, and the level of malondialdehyde (MDA) (a product of lipid peroxidation), was measured at 0, 5, 10, 15, and 30 min of incubation.
32(0,1,1,2) Details
9217305 Hitzfeld B, Friedrichs KH, Ring J, Behrendt H: Airborne particulate matter modulates the production of reactive oxygen species in human polymorphonuclear granulocytes. Toxicology. 1997 Jul 11;120(3):185-95.

The effects of the PM extracts were inhibited by superoxide dismutase (SOD), catalase and sodium azide (NaN3).
31(0,1,1,1) Details
11790383 Shahidullah M, Duncan A, Strachan PD, Rafique KM, Ball SL, McPate MJ, Nelli S, Martin W: Role of catalase in the smooth muscle relaxant actions of sodium azide and cyanamide. Eur J Pharmacol. 2002 Jan 18;435(1):93-101.

Moreover, results obtained using a difference spectrophotometric assay based upon the oxidation of haemoglobin were consistent with the catalase-dependent oxidation of sodium azide to nitric oxide (NO) and of cyanamide to nitroxyl anion.
93(1,1,3,3) Details
16728955 Kang YS, Lee DH, Yoon BJ, Oh DC: Purification and characterization of a catalase from photosynthetic bacterium Rhodospirillum rubrum S1 grown under anaerobic conditions. Am J Physiol Lung Cell Mol Physiol. 2005 May;288(5):L903-9. Epub 2005 Jan 7.

Sodium cyanide, sodium azide, and hydroxylamine, all of which are known heme protein inhibitors, inhibited catalase activity by 50% at concentrations of 11.5 microM, 0.52 microM, and 0.11 microM, respectively.
89(1,1,1,9) Details
17512464 Tintinger GR, Theron AJ, Potjo M, Anderson R: Reactive oxidants regulate membrane repolarization and store-operated uptake of calcium by formyl peptide-activated human neutrophils. Chem Biol Interact. 2008 Nov 25;176(2-3):129-36. Epub 2008 Aug 5.

In the current study, we have investigated the effects of superoxide dismutase (SOD), catalase, methionine, and the myeloperoxidase (MPO) inhibitors, sodium azide and 4-aminobenzoyl hydrazide (ABAH), as well as those of H (2) O (2) and HOCl (both at 100 microM) on the alterations in membrane potential which accompany activation of human neutrophils with the chemoattractant, FMLP (1 microM), and on store-operated uptake of Ca (2+).
87(1,1,2,2) Details
7592539 Itoh M, Nakamura M, Suzuki T, Kawai K, Horitsu H, Takamizawa K: Mechanism of chromium (VI) toxicity in Escherichia coli: is hydrogen peroxide essential in Cr (VI) toxicity?. Chem Biol Interact. 1996 Dec 20;102(3):133-53.

Bacterial cells were incubated for 1 h with shaking in the presence of Cr (VI), hydrogen peroxide, sodium azide as catalase inhibitor, and/or mannitol as radical scavenger.
32(0,1,1,2) Details
9502580 Hasegawa H, Suzuki K, Nakaji S, Sugawara K: Analysis and assessment of the capacity of neutrophils to produce reactive oxygen species in a 96-well microplate format using lucigenin- and luminol-dependent chemiluminescence. Environ Health Perspect. 2004 Apr;112(5):553-6.

Furthermore, we studied the contribution of various ROS to LgCL and luminol-dependent CL (LmCL) using modulators of ROS metabolism including superoxide dismutase (SOD), catalase, deferoxamine and sodium azide (NaN3).
31(0,1,1,1) Details
11563540 Elleder M, Borovansky J: Autofluorescence of melanins induced by ultraviolet radiation and near ultraviolet light. Platelets. 2000 Aug;11(5):278-85.

It was inhibited by anhydrous conditions, sodium azide and catalase.
31(0,1,1,1) Details
8593088 Petrenko IuM, Titov VIu, Vladimirov IuA: [The property of tetracyclines to induce methemoglobin formation in erythrocytes and to inactivate catalase when exposed to radiation in the visible range]. Antibiot Khimioter. 1995 Jun;40(6):10-8.

When tetracycline and chlortetracycline were incubated an a dark room in the presence of erythrocytes with erythrocytic catalase completely inactivated by sodium azide, the antibiotics induced methemoglobin formation in them.
87(1,1,1,7) Details
16716939 Kobayashi I, Tamura T, Sghaier H, Narumi I, Yamaguchi S, Umeda K, Inagaki K: Characterization of monofunctional catalase KatA from radioresistant bacterium Deinococcus radiodurans. J Biolumin Chemilumin. 1994 Mar-Apr;9(2):79-86.

The catalase activity of KatA was inhibited by sodium azide, sodium cyanide and 3-amino-1,2,4-triazole.
86(1,1,1,6) Details
16951741 Kambayashi Y, Hitomi Y, Kodama N, Kubo M, Okuda J, Takemoto K, Shibamori M, Takigawa T, Ogino K: pH profile of cytochrome c-catalyzed tyrosine nitration. Arch Toxicol. 1995;69(7):498-504.

The cytochromec-catalyzed nitration of tyrosine was inhibited by catalase, sodium azide, cystein, and uric acid.
31(0,1,1,1) Details
9989945 Kagawa M, Murakoshi N, Nishikawa Y, Matsumoto G, Kurata Y, Mizobata T, Kawata Y, Nagai J: Purification and cloning of a thermostable manganese catalase from a thermophilic bacterium. Acta Pol Pharm. 1996 Sep-Oct;53(5):357-9.

The catalase was determined to be a manganese catalase, based on results from atomic absorption spectra and inhibition experiments using sodium azide.
84(1,1,1,4) Details
10967081 Kortuem K, Geiger LK, Levin LA: Differential susceptibility of retinal ganglion cells to reactive oxygen species. Biochem Biophys Res Commun. 1999 Sep 24;263(2):392-7.

Aminotriazole, L-buthionine sulfoximine, and sodium azide partly abrogated the RGC resistance to oxidative stress, suggesting that this resistance may be mediated by catalase and/or glutathione peroxidase.
82(1,1,1,2) Details
9415210 Ejchart A, Chlopkiewicz B: Characteristics of mutagenesis by bleomycin and adriamycin in Salmonella typhimurium: action of catalase. Cancer Lett. 1998 Jan 9;122(1-2):9-15.

The activity of catalase in bacterial cells was inhibited by sodium azide.
83(1,1,1,3) Details
19778251 Sarkar C, Mitra PK, Saha S, Nayak C, Chakraborty R: Effect of copper-hydroquinone complex on oxidative stress-related parameters in human erythrocytes (in vitro). Chem Res Toxicol. 2003 Apr;16(4):524-30.

Catalase inhibition by sodium azide depleted reduced glutathione level further.
82(1,1,1,2) Details
19055648 Janousek SJ, Rosa L, Janousek S, Jirova D, Kejlova K: Oxidative stress may modify zinc protoporphyrin/heme ratio in hematofluorometry. Psychopharmacology. 2008 Nov;200(4):455-64. Epub 2008 Jun 30.

Washed red blood cells (RBCs), supplemented or non-supplemented with sodium azide (to inhibit catalase activity), were exposed to different concentrations of hydrogen peroxide as well as ascorbic acid.
82(1,1,1,2) Details
18164679 Jeanjean R, Latifi A, Matthijs HC, Havaux M: The PsaE subunit of photosystem I prevents light-induced formation of reduced oxygen species in the cyanobacterium Synechocystis sp. Biochim Biophys Acta. 2008 Mar;1777(3):308-16. Epub 2007 Dec 5.

When catalases were inhibited by sodium azide, the production of reactive oxygen species was enhanced in DeltapsaE relative to WT.
82(1,1,1,2) Details
15062877 Komarov AM, Hall JM, Weglicki WB: Azidothymidine promotes free radical generation by activated macrophages and hydrogen peroxide-iron-mediated oxidation in a cell-free system. FEBS Lett. 2002 Jul 17;523(1-3):128-32.

Latex-activated cells oxidize DCDHF extracellularly due to release of hydrogen peroxide and low-molecular iron complexes, which is verified using catalase, desferal and the peroxidase inhibitor sodium azide.
82(1,1,1,2) Details
12581189 Amer J, Goldfarb A, Fibach E: Flow cytometric measurement of reactive oxygen species production by normal and thalassaemic red blood cells. Biochim Biophys Acta. 1999 Sep 21;1421(1):131-9.

The latter effect is most likely related to H2O2 decomposition by catalase as both sodium azide, an antimetabolite that inhibits catalase and low temperature increased the fluorescence of stimulated RBCs.
81(1,1,1,1) Details
11236840 Salmela KS, Tsyrlov IB, Lieber CS: Azide inhibits human cytochrome P -4502E1, 1A2, and 3A4. Kidney Int. 1994 Oct;46(4):1025-30.

When MEOS activity is measured, sodium azide commonly is used to block the contaminating catalase.
81(1,1,1,1) Details
8533604 Mueller S, Arnhold J: Fast and sensitive chemiluminescence determination of H2O2 concentration in stimulated human neutrophils. Biochem Mol Biol Int. 1995 May;36(1):227-32.

Concentrations of H2O2 were diminished by catalase and enhanced by sodium azide owing to inhibition of cellular catalase and myeloperoxidase.
81(1,1,1,1) Details
7750790 Rohn TT, Hinds TR, Vincenzi FF: Inhibition by activated neutrophils of the Ca2+ pump ATPase of intact red blood cells. Free Radic Biol Med. 1995 Apr;18(4):655-67.

The addition of sodium azide, a potent inhibitor of endogenous RBC catalase, enhanced inhibition of the Ca2+ pump ATPase of intact RBCs.
81(1,1,1,1) Details
8179017 Cohn LA, Kinnula VL, Adler KB: Antioxidant properties of guinea pig tracheal epithelial cells in vitro. ScientificWorldJournal. 2004 Jun 29;4:490-9.

Inhibition of catalase (Cat) with sodium azide (NaAz) significantly attenuated the ability of GPTE cells to remove higher concentrations of H2O2.
81(1,1,1,1) Details
9098086 Frati E, Khatib AM, Front P, Panasyuk A, Aprile F, Mitrovic DR: Degradation of hyaluronic acid by photosensitized riboflavin in vitro. Free Radic Biol Med. 1997;22(7):1139-44.

A decrease of HA viscosity occurs in PO (4)-buffered solutions and is accelerated by high pH, Fe2+ (but much less so by Fe3+), certain metal chelators, and horseradish peroxidase (HRP); it is partially inhibited by catalase and less so by superoxide dismutase (SOD).
The reactivity of the system was completely blocked by Tris, ethanol, aspirin, d-manitol, dimethylthiourea (DMTU), dimethylsulfoxide (DMSO), and sodium azide.
2(0,0,0,2) Details
15052604 Mazzio EA, Soliman KF: Glioma cell antioxidant capacity relative to reactive oxygen species produced by dopamine. Free Radic Biol Med. 1997;23(7):980-5.

Preincubation with sodium azide but not buthionine-[S, R]-sulfoximine attenuated this response, indicating catalase as the primary enzyme responsible for this effect.
The glioma catalase reaction rate was slightly attenuated by exposure to LPS/IFN-g for 24 h.
2(0,0,0,2) Details
17302992 Wang ZJ, Liang CL, Li GM, Yu CY, Yin M: Stearic acid protects primary cultured cortical neurons against oxidative stress. Free Radic Res. 1998 Jul;29(1):25-34.


Endogenous antioxidant enzymes activity [superoxide dismutases (SOD), glutathione peroxidase (GSH-Px), and catalase (CAT)] and lipid peroxidation in cultured cortical neurons were evaluated using commercial kits. {3-[1 (p-chlorobenzyl)- 5-(isopropyl)-3-t-butylthiondol-2-yl]-2,2-dimethylpropanoic acid, Na} [MK886; 5 micromol/L; a noncompetitive inhibitor of proliferator-activated receptor (PPAR) alpha], bisphenol A diglycidyl ether (BADGE; 100 micromol/L; an antagonist of PPAR gamma), and cycloheximide (CHX; 30 micromol/L, an inhibitor of protein synthesis) were tested for their effects on the neuroprotection afforded by stearic acid.
1(0,0,0,1) Details
9923964 Menon M, Maramag C, Malhotra RK, Seethalakshmi L: Effect of vitamin C on androgen independent prostate cancer cells (PC3 and Mat-Ly-Lu) in vitro: involvement of reactive oxygen species-effect on cell number, viability and DNA synthesis. Free Radic Biol Med. 1999 Jul;27(1-2):127-33.

Ascorbate induced these changes through the production of hydrogen peroxide since addition of catalase (100-300 units/ml), an enzyme that degrades hydrogen peroxide, inhibited the effects of ascorbate on these cell lines.
That singlet oxygen scavengers such as sodium azide and hydroquinone, hydroxyl radical scavengers such as D-mannitol and DL-alpha-tocopherol did not counteract the effects of ascorbate on thymidine incorporation suggests that these free radicals are not involved in cellular damage.
1(0,0,0,1) Details
7753758 Takeyama Y, Ogino K, Segawa H, Kobayashi H, Uda T, Houbara T: Effects of zinc on production of active oxygen species by rat neutrophils. . FEMS Microbiol Lett. 1999 Apr 15;173(2):285-90.

Zinc at concentrations lower than 0.1 mM augmented the intensity of chemiluminescence and showed a bimodal pattern, the first peak of which was inhibited by superoxide dismutase and catalase, while the second peak disappeared in the presence of catalase, but was unaffected by superoxide dismutase.
Homogenized neutrophils showed a bimodal pattern on induction by zinc, the second peak of which was inhibited slightly by catalase and completely by sodium azide, but was not inhibited by superoxide dismutase.
1(0,0,0,1) Details
9566705 Sahu SC, Eppley RM, Page SW, Gray GC, Barton CN, O'Donnell MW: Peroxidation of membrane lipids and oxidative DNA damage by fumonisin B1 in isolated rat liver nuclei. J Leukoc Biol. 1999 Feb;65(2):196-204.

In addition, the active oxygen scavengers catalase, superoxide dismutase (SOD), mannitol and sodium azide had no significant inhibitory effects on the FB1-induced DNA strand breaks.
However, a small but significant reduction in lipid peroxidation by catalase and mannitol was observed.
1(0,0,0,1) Details
8179634 Park JW, Kim HK: Strand scission in DNA induced by S-nitrosothiol with hydrogen peroxide. Enzyme Microb Technol. 2000 Dec;27(10):789-792.


Sodium azide and mannitol inhibited S-nitrosothiol/H2O2-induced strand breaks in DNA.
0(0,0,0,0) Details
10660661 Yamada M, Suzuki K, Kudo S, Totsuka M, Simoyama T, Nakaji S, Sugawara K: Effect of exhaustive exercise on human neutrophils in athletes. ScientificWorldJournal. 2004 Sep 2;4:785-94.


Just after exercise, the LgCL response was not affected, while the response of LmCL mixed with sodium azide, which inhibits catalase and myeloperoxidase (MPO) activity, was significantly enhanced (p < 0.05).
0(0,0,0,0) Details
8831581 Haber PS, Gentry RT, Mak KM, Mirmiran-Yazdy SA, Greenstein RJ, Lieber CS: Metabolism of alcohol by human gastric cells: relation to first-pass metabolism. Drug Metabol Drug Interact. 1999;15(4):239-58.


Acetate production was inhibited by 4-methylpyrazole (a class I alcohol dehydrogenase [ADH] inhibitor) and by m-nitrobenzaldehyde (a selective substrate for class IV ADH isoenzyme) but not by sodium azide (a catalase inhibitor).
0(0,0,0,0) Details
10826924 Kim RH, Park JE, Park JW: Ceruloplasmin enhances DNA damage induced by hydrogen peroxide in vitro. Free Radic Res. 2000 Jul;33(1):81-9.

The capacity of Cp to enhance oxidative damage to DNA was inhibited by hydroxyl radical scavengers such as sodium azide and mannitol, a metal chelator, diethylenetriaminepentaacetic acid, and catalase.
31(0,1,1,1) Details
7867972 Karuzina II, Archakov AI: Hydrogen peroxide-mediated inactivation of microsomal cytochrome P450 during monooxygenase reactions. J Toxicol Environ Health A. 2009;72(6):369-73.

The acceleration of cytochrome P450 loss in the presence of catalase inhibitors (sodium azide, hydroxylamine) indicates that hydrogen peroxide is involved in hemoprotein degradation.
31(0,1,1,1) Details
8743726 Pyzhova NS, Nikandrov VN, Nikandrov NN: Effect of active oxygen species scavengers on fibrinolytic activity of some proteinases. Thromb Res. 1996 May 15;82(4):303-12.

Singlet oxygen scavengers change proteinase activity insignificantly except for strong inhibition of pepsin and papain by sodium azide, but pepsin-by histidine, and fibrinolytic urokinase activity-by all used O2 delta 1 scavengers.
Catalase changed proteinase activity insignificantly, though it leads to total inhibition of pepsin activity at final 4.5 x 10 (-4) M concentration.
1(0,0,0,1) Details
8055842 Ishizaki T, Yano E, Urano N, Evans PH: Crocidolite-induced reactive oxygen metabolites generation from human polymorphonuclear leukocytes. Neurosci Lett. 2005 Mar 7;376(1):66-70. Epub 2004 Dec 16.

Superoxide dismutase, catalase, and dimethyl sulfoxide, which are scavengers of O2-, H2O2, and OH., respectively, inhibited the production of crocidolite-stimulated CL from PMN, also in a dose-dependent manner.
Sodium azide, an inhibitor of myeloperoxidase (MPO) to produce OCl-, also inhibited CL production.
1(0,0,0,1) Details
9665739 Liu Z, Lu Y, Rosenstein B, Lebwohl M, Wei H: Benzo [a] pyrene enhances the formation of 8-hydroxy-2'-deoxyguanosine by ultraviolet A radiation in calf thymus DNA and human epidermoid carcinoma cells. Chem Res Toxicol. 2006 May;19(5):719-28.


The results showed that only superoxide dismutase and genistein significantly quenched BaP plus UVA-induced 8-OHdG, whereas catalase, sodium azide, and mannitol exhibited no effect.
0(0,0,0,0) Details
8598491 Hansson M, Asea A, Ersson U, Hermodsson S, Hellstrand K: Induction of apoptosis in NK cells by monocyte-derived reactive oxygen metabolites. Gastroenterology. 1996 Oct;111(4):863-70.


Sodium azide, a myeloperoxidase inhibitor, substantially reduced the monocyte-induced apoptosis in NK cells.
0(0,0,0,0) Details
9557922 Lacy F, O'Connor DT, Schmid-Schonbein GW: Plasma hydrogen peroxide production in hypertensives and normotensive subjects at genetic risk of hypertension. Mol Cell Biochem. 1993 Sep 22;126(2):125-33.

METHODS: An electrode technique was used to determine plasma hydrogen peroxide levels after blockade of endogenous catalase with sodium azide.
31(0,1,1,1) Details
10677150 Lucchi L, Bergamini S, Botti B, Rapana R, Ciuffreda A, Ruggiero P, Ballestri M, Tomasi A, Albertazzi A: Influence of different hemodialysis membranes on red blood cell susceptibility to oxidative stress. Bioorg Khim. 2008 Sep-Oct;34(5):654-60.

RBC were incubated with t-butyl hydroperoxide as an oxidizing agent both in the presence and in the absence of the catalase inhibitor sodium azide.
31(0,1,1,1) Details
14743538 Koval' OA, Boguslavskii EG, Oleinikova SB, Chernolovskaia EL, Litvak VV, Nadolinnyi VA, Blasov VV: [Copper-catalyzed cleavage of DNA by arenes] . Free Radic Biol Med. 2007 Jun 15;42(12):1851-7. Epub 2007 Mar 24.

Catalase, sodium azide, and bathocuproine, which is a specific chelator of Cu (I), completely inhibit the reaction.
31(0,1,1,1) Details
18422880 Daghastanli NA, Itri R, Baptista MS: Singlet oxygen reacts with 2',7'-dichlorodihydrofluorescein and contributes to the formation of 2',7'-dichlorofluorescein. Photochem Photobiol. 2008 Sep-Oct;84(5):1238-43. Epub 2008 Apr 12.

By carefully preparing solutions in which (1) O (2) is quantitatively generated in the presence of DCFH, we were able to show that the formation rate of the fluorescent molecule derived from DCFH oxidation, which is 2',7'-dichlorofluorescein (DCF), increases in D (2) O and decreases in sodium azide, proving the direct role of (1) O (2) in this process.
The absence of any effect of SOD and catalase ruled out the DCFH oxidation by O (2)(-), indicating that both (1) O (2) and MB (2+) react with DCFH.
1(0,0,0,1) Details
8526746 Lee TC, Ho IC: Modulation of cellular antioxidant defense activities by sodium arsenite in human fibroblasts. Life Sci. 1999;65(20):2135-42.

Sodium arsenite-enhanced heme oxygenase synthesis was inhibited by co-treatment of cells with the antioxidants sodium azide and dimethyl sulfoxide.
Sodium arsenite toxicity was partly reduced by addition of catalase to the culture medium.
1(0,0,0,1) Details
12703969 Yazzie M, Gamble SL, Civitello ER, Stearns DM: Uranyl acetate causes DNA single strand breaks in vitro in the presence of ascorbate (vitamin C). Arch Biochem Biophys. 1999 Feb 15;362(2):346-55.


Plasmid relaxation was inhibited by coincubation of reactions with catalase but not by coincubation with the radical scavengers mannitol, sodium azide, or 5,5-dimethyl-1-pyrroline-N-oxide.
0(0,0,0,0) Details
8397140 Rathakrishnan C, Tiku ML: Lucigenin-dependent chemiluminescence in articular chondrocytes. . Free Radic Biol Med. 1993 Aug;15(2):143-9.


Catalase and the metabolic inhibitor, sodium azide, which inhibits the enzyme myeloperoxidase, had no inhibitory effect on lucigenin-dependent chemiluminescence production.
0(0,0,0,0) Details
9021167 Tsou TC, Yang JL: Formation of reactive oxygen species and DNA strand breakage during interaction of chromium (III) and hydrogen peroxide in vitro: evidence for a chromium (III)-mediated Fenton-like reaction. Alcohol Clin Exp Res. 2006 Sep;30(9):1500-5.

Sodium azide, D-mannitol, Tris-HCl, or catalase completely inhibited Cr (III)/H2O2-induced DNA breakage, but superoxide dismutase did not.
31(0,1,1,1) Details
8951230 Oakley GG, Devanaboyina U, Robertson LW, Gupta RC: Oxidative DNA damage induced by activation of polychlorinated biphenyls (PCBs): implications for PCB-induced oxidative stress in breast cancer. Artif Organs. 2000 Jan;24(1):1-6.

The addition of catalase (100 U/mL) and sodium azide (0.1 M) reduced the effect of CuCl (2) (849 and 896 8-oxodG/10 (6) nucleotides, respectively), while superoxide dismutase (600 U/mL) moderately stimulated and glutathione (100 microM) substantially stimulated 8-oxodG formation (3014 and 4415 8-oxodG/10 (6) nucleotides, respectively).
31(0,1,1,1) Details
11118588 Gligic L, Radulovic Z, Zavisic G: Superoxide dismutase biosynthesis by two thermophilic bacteria. Br J Pharmacol. 1995 Dec;116(8):3302-8.

In addition to superoxide dismutase (SOD; EC 1.15.1.1), qualitative analyses demonstrated the presence of catalase (EC 1.11.1.6), peroxidases and oxidases in both bacterial strains.
A slight decrease of SOD activity observed in the presence of 0.3 M potassium cyanide and its complete insensitivity to hydrogen peroxide (5 mM) and sodium azide (20 mM) action suggest that the enzyme occurring in the two thermophiles represents Mn SOD.
1(0,0,0,1) Details
11332879 Petersen AB, Gniadecki R, Vicanova J, Thorn T, Wulf HC: Hydrogen peroxide is responsible for UVA-induced DNA damage measured by alkaline comet assay in HaCaT keratinocytes. J Photochem Photobiol B. 2000 Dec;59(1-3):123-31.

Singlet oxygen (1O2) did not seem to play an important role in the UVA-induced DNA-damage since the specific 1O2 scavenger sodium azide (NaN3) and the less specific 1O2 scavenger beta-carotene did not markedly prevent either DNA-damage or H2O2 production.
Increasing the intracellular levels of H2O2 with aminotriazole (AT) (a catalase blocker) and buthionine sulfoximine (BSO) (an inhibitor of glutathione synthesis) potentiated the UVA-induced DNA damage.
1(0,0,0,1) Details
8960159 Nagai F, Okubo T, Ushiyama K, Satoh K, Kano I: Formation of 8-hydroxydeoxyguanosine in calf thymus DNA treated with tert-butylhydroquinone, a major metabolite of butylated hydroxyanisole. J Biomed Mater Res A. 2005 Jul 1;74(1):1-12.


This effect was strongly enhanced by CuCl2 and suppressed by EDTA, bathocuproinedisulfonic acid disodium salt, methionine, glutathione reduced form or catalase, but was not affected by mannitol, sodium benzoate or sodium azide.
0(0,0,0,0) Details
9188807 Ali MK, Tayyab S: Calcium-induced bilirubin-dependent hemolysis of human erythrocytes. . J Immunol. 1996 Jan 1;156(1):42-7.


Involvement of activated oxygen species in hemolytic process seems to be unlikely as inclusion of sodium azide and catalase did not prevent hemolysis.
0(0,0,0,0) Details
7728964 Nagai F, Ushiyama K, Satoh K, Kasai H, Kano I: Formation of 8-hydroxydeoxyguanosine in calf thymus DNA treated in vitro with phenylhydroquinone, the major metabolite of O-phenylphenol. Chem Res Toxicol. 2002 Aug;15(8):1017-22.

The formation of 8OHdG by PHQ was reduced by oxygen radical scavengers such as catalase, sodium benzoate and sodium azide.
31(0,1,1,1) Details
7673115 Gergel D, Misik V, Ondrias K, Cederbaum AI: Increased cytotoxicity of 3-morpholinosydnonimine to HepG2 cells in the presence of superoxide dismutase. J Biol Chem. 1995 Sep 8;270(36):20922-9.

Catalase abolished, while sodium azide potentiated, this toxicity, suggesting a key role for H2O2 in the overall mechanism.
31(0,1,1,1) Details
11342285 Dincer A, Aydemir T: Purification and characterization of catalase from chard (Beta vulgaris var. cicla). Am J Respir Cell Mol Biol. 2010 Mar 4.

9(0,0,0,9) Details
10976731 Ball BA, Gravance CG, Medina V, Baumber J, Liu IK: Catalase activity in equine semen. Am J Vet Res. 2000 Sep;61(9):1026-30.

8(0,0,0,8) Details
12916153 Semchyshyn HM, Dyl'ovyi MV, Lushchak VI: [pH-dependency of Escherichia coli catalase activity under modified culture conditions]. Ukr Biokhim Zh. 2002 Sep-Oct;74(5):34-41.

7(0,0,0,7) Details
7833505 Demiryurek AT, Wainwright CL, Wadsworth RM, Kane KA: Characterization of a method for the detection of drugs with free radical scavenging activity using porcine leukocytes. J Pharmacol Toxicol Methods. 1994 Sep;32(1):35-40.

Superoxide dismutase (0.1 units/mL) and catalase (50 units/mL) inhibited X-XO, but they were ineffective in leukocyte suspensions except at concentrations 500 times and 20 times higher.
Sodium azide (10 (-5) to 10 (-3) M) caused a marked inhibition in CL production in activated leukocytes, but not of X-XO CL.
1(0,0,0,1) Details
15346198 Wang BZ, Wei XB, Liu WY: Cleavage of supercoiled circular double-stranded DNA induced by a eukaryotic cambialistic superoxide dismutase from Cinnamomum camphora. Free Radic Biol Med. 1998 Oct;25(6):720-7.


The supercoiled DNA-cleaving activity of the cambialistic SOD can be inhibited by either SOD inhibitor (azide) or catalase and hydroxyl radical scavengers (ethanol and mannitol).
1(0,0,0,1) Details
10443929 Liu Z, Lu Y, Lebwohl M, Wei H: PUVA (8-methoxy-psoralen plus ultraviolet A) induces the formation of 8-hydroxy-2'-deoxyguanosine and DNA fragmentation in calf thymus DNA and human epidermoid carcinoma cells. Toxicol Lett. 1996 Dec 16;89(2):163-7.


The results showed that only sodium azide and genistein significantly quenched PUVA-induced 8-OHdG, whereas catalase, superoxide dismutase, and mannitol exhibited no effect.
0(0,0,0,0) Details
15640286 Dauletbaev N, Rickmann J, Viel K, Diegel H, von Mallinckrodt C, Stein J, Wagner TO, Bargon J: Antioxidant properties of cystic fibrosis sputum. Acta Pharmacol Sin. 2007 Mar;28(3):315-26.


The H (2) O (2)-detoxifying potential of CF sputum was sustained after catalase and heme peroxidases were inactivated by sodium azide, which does not affect glutathione peroxidase.
0(0,0,0,0) Details
19060940 Kosenko EA, Solomadin IN, Marov NV, Venediktova NI, Pogosian AS, Kaminskii IuG: [Role of glycolysis and antioxidant enzymes in the toxicity of amyloid beta peptide Abeta25-35 to erythrocytes]. Cancer Lett. 1994 Oct 14;85(2):159-64.


Sodium azide, a catalase inhibitor, did not affect the cell lysis under the action of Abeta (25-35) .
0(0,0,0,0) Details
10764744 Bai J, Cederbaum AI: Overexpression of catalase in the mitochondrial or cytosolic compartment increases sensitivity of HepG2 cells to tumor necrosis factor-alpha-induced apoptosis. J Biol Chem. 1997 Nov 14;272(46):28962-70.

Sodium azide, an inhibitor of catalase, reduced the increased sensitivity of mC5 and C33 cells to TNF-alpha to the level of toxicity found with control Hp cells.
7(0,0,0,7) Details
12029047 Amo T, Atomi H, Imanaka T: Unique presence of a manganese catalase in a hyperthermophilic archaeon, Pyrobaculum calidifontis VA1. Biochemistry. 1998 Jul 14;37(28):10307-12.

In contrast to typical heme catalases, the catalase was not strongly inhibited by sodium azide.
7(0,0,0,7) Details
17983766 Ebara S, Shigemori Y: Alkali-tolerant high-activity catalase from a thermophilic bacterium and its overexpression in Escherichia coli. Protein Expr Purif. 2008 Feb;57(2):255-60. Epub 2007 Oct 1.

7(0,0,0,7) Details
10951218 Beghetto C, Renken C, Eriksson O, Jori G, Bernardi P, Ricchelli F: Implications of the generation of reactive oxygen species by photoactivated calcein for mitochondrial studies. Arch Biochem Biophys. 1994 Jul;312(1):285-91.

The photodegradation of histidine was mainly mediated by singlet oxygen (1O2), as shown by the inhibitory effect of sodium azide, a specific 1O2 scavenger.
In addition to 1O2, hydroxyl radicals and hydrogen peroxide were involved as reactive species, as shown by using mannitol and catalase as scavengers.
1(0,0,0,1) Details
7814397 Sakuraba H, Noguchi T: Alcohol:NAD+ oxidoreductase is present in rat liver peroxisomes. . J Biol Chem. 1995 Jan 6;270(1):37-40.


The enzyme activity was not affected by pyrazole, an inhibitor of alcohol dehydrogenase and sodium azide, an inhibitor of catalase.
0(0,0,0,0) Details
16447283 Bizzozero OA, Ziegler JL, De Jesus G, Bolognani F: Acute depletion of reduced glutathione causes extensive carbonylation of rat brain proteins. J Microbiol. 2006 Apr;44(2):185-91.


Inhibition of catalase activity with sodium azide and aminotriazole, and glutathione peroxidase activity with mercaptosuccinic acid did not increase PCOs or TBARS, suggesting that increased production of reactive oxygen species (ROS) rather than compromised cellular antioxidant defenses is the cause for the accumulation of H2O2 after GSH depletion.
0(0,0,0,0) Details
9583081 Takayama F, Egashira T, Yamanaka Y: [Assay for oxidative stress injury by detection of luminol-enhanced chemiluminescence in a freshly obtained blood sample: a study to follow the time course of oxidative injury]. Nippon Yakurigaku Zasshi. 1998 Mar;111(3):177-86.

This CL was weakened slightly by superoxide dismutase and catalase, but markedly decreased by sodium azide. 2.
6(0,0,1,1) Details
11030462 Jancinova V, Drabikova K, Nosal R, Danihelova E: Platelet-dependent modulation of polymorphonuclear leukocyte chemiluminescence. Eur J Haematol. 2003 Feb;70(2):84-90.

Superoxide dismutase with catalase and sodium azide were used, respectively, to differentiate the intracellular and the extracellular part of the chemiluminescence signal.
6(0,0,1,1) Details
16844094 Pereira A, Dean B: Clozapine bioactivation induces dose-dependent, drug-specific toxicity of human bone marrow stromal cells: a potential in vitro system for the study of agranulocytosis. Biochem Pharmacol. 2006 Sep 14;72(6):783-93. Epub 2006 Jul 17.

Exogenous GSH, N-acetylcysteine, l-ascorbic acid, catalase, and sodium azide afforded protection to cells whereas S-methylGSH, GSSG, ketoprofen and proadifen did not.
6(0,0,1,1) Details
16696575 Park JH, Troxel AB, Harvey RG, Penning TM: Polycyclic aromatic hydrocarbon (PAH) o-quinones produced by the aldo-keto-reductases (AKRs) generate abasic sites, oxidized pyrimidines, and 8-oxo-dGuo via reactive oxygen species. Luminescence. 2000 Jan-Feb;15(1):15-20.

In the presence of Cu (II)-mediated PAH o-quinone redox-cycling, catalase completely suppressed the formation of the lesions, but mannitol and sodium benzoate were without effect.
By contrast, sodium azide, which acts as a *OH and 1O2 scavenger, inhibited the formation of all oxidative lesions, suggesting that the ROS responsible was 1O2.
1(0,0,0,1) Details
16144060 McBane J, Santerre P, Labow R: Role of protein kinase C in the monocyte-derived macrophage-mediated biodegradation of polycarbonate-based polyurethanes. Gut. 1996 Sep;39(3):407-15.


MDM-mediated degradation was assessed by radiolabel release in the presence of a PKC activator (phorbol myristate acetate), inhibitor (H7), and a catalase/peroxidase inhibitor (NaN3).
1(0,0,0,1) Details
12727198 Afzal M, Matsugo S, Sasai M, Xu B, Aoyama K, Takeuchi T: Method to overcome photoreaction, a serious drawback to the use of dichlorofluorescin in evaluation of reactive oxygen species. Biochem Biophys Res Commun. 2003 May 16;304(4):619-24.


Although reactive oxygen species scavengers, such as catalase, superoxide dismutase, and sodium azide, did not suppress the increase in non-specified fluorescence, reagents such as ascorbic acid, mercaptopropionyl glycine, and methoxycinnamic acid, in a cell-free system, almost completely suppressed it with little effect on the fluorescence of DCF.
0(0,0,0,0) Details
8675397 Giangiacomo A, Olesen PR, Ortwerth BJ: Ascorbic acid and glucose oxidation by ultraviolet A-generated oxygen free radicals. Neuropsychopharmacology. 2006 May;31(5):997-1008.

The role of individual reactive oxygen species was determined by the protective effects of superoxide dismutase, catalase, and sodium azide.
6(0,0,1,1) Details
8949646 Millar AD, Rampton DS, Chander CL, Claxson AW, Blades S, Coumbe A, Panetta J, Morris CJ, Blake DR: Evaluating the antioxidant potential of new treatments for inflammatory bowel disease using a rat model of colitis. 198-9.

RESULTS: The model was validated by demonstrating that the profile of effects on chemiluminescence of acetic acid induced colitis biopsy specimens given by conventional antioxidants (sodium azide, catalase, copper-zinc superoxide dismutase, dimethyl sulphoxide, N-acetylcysteine and ascorbate) and standard therapies (5-aminosalicylate and hydrocortisone) resembled that previously reported using biopsy specimens from ulcerative colitis.
6(0,0,1,1) Details
8395887 Leteurtre F, Fesen M, Kohlhagen G, Kohn KW, Pommier Y: Specific interaction of camptothecin, a topoisomerase I inhibitor, with guanine residues of DNA detected by photoactivation at 365 nm. Biochimie. 2001 Jun;83(6):487-95.

In aerobic conditions, the most effective scavengers were thiourea, sodium azide, and catalase.
6(0,0,1,1) Details
20203294 Ranzato E, Biffo S, Burlando B: Selective Ascorbate Toxicity to Malignant Mesothelioma: A Redox Trojan Mechanism. Acta Biochim Biophys Sin. 2004 Sep;36(9):609-17.

Ascorbate transport inhibitors phloretin, sodium azide and ouabain did not reduce ascorbate toxicity .
Toxicity was markedly reduced by the H2O2-degrading enzyme catalase.
1(0,0,0,1) Details
9733019 Becker TW, Krieger G, Witte I: Different DNA damaging species as a result of oxidation of n-butyraldehyde and iso-butyraldehyde by Cu (II). Life Sci. 1998;63(8):645-57.

While catalase and neocuproine inhibited strand break formation induced by iso-BuA/Cu (II) to a high degree, these inhibitors were less effective in the n-BuA/Cu (II) reaction.
On the other hand, sodium azide showed a high strand break inhibition in the n-BuA/Cu (II) reaction, but low inhibition in the iso-BuA/Cu (II) reaction. 2-Deoxyguanosine was hydroxylated in the 8-position by iso-BuA/Cu (II) but little reaction occurred with n-BuA/Cu (II).
1(0,0,0,1) Details
9794700 Haber PS, Apte MV, Applegate TL, Norton ID, Korsten MA, Pirola RC, Wilson JS: Metabolism of ethanol by rat pancreatic acinar cells. J Biosci Bioeng. 2006 Apr;101(4):315-21.


Phenanthroline (an inhibitor of classes I through III isoenzymes of alcohol dehydrogenase (ADH)) inhibited pancreatic ethanol oxidation by 90%, but 4-methylpyrazole (a class I and II ADH inhibitor), carbon monoxide (a cytochrome P450 inhibitor), and sodium azide (a catalase inhibitor) had no effect.
0(0,0,0,0) Details
12691870 Walrand S, Valeix S, Rodriguez C, Ligot P, Chassagne J, Vasson MP: Flow cytometry study of polymorphonuclear neutrophil oxidative burst: a comparison of three fluorescent probes. J Neurosci Res. 2006 Mar;83(4):656-67.


Cell suspensions were then split for each probe into five different aliquots containing either no effector or one effector: N-ethylmaleimide (NEM, 150 micro mol/l, NADPH oxidase inhibitor), sodium azide (NaN (3), 50 micro mol/l, peroxidase and catalase inhibitor), N-nitro-L-arginine methyl ester (L-NAME, 1.5 micro mol/l, NO (z.rad;) synthase inhibitor) or H (2) O (2) (30%).
0(0,0,0,0) Details
10561478 Ohyashiki T, Nunomura M, Katoh T: Detection of superoxide anion radical in phospholipid liposomal membrane by fluorescence quenching method using 1,3-diphenylisobenzofuran. Alcohol Clin Exp Res. 1998 Aug;22(5):1113-9.


On the other hand, catalase (1 U/ml), and hydroxyl radical and singlet oxygen scavengers (10 mM sodium benzoate, 300 mM mannitol, 1 mM tryptophan and 1 mM sodium azide) did not protect xanthine/xanthine oxidase-induced fluorescence quenching of DPBF-labeled liposomes.
0(0,0,0,0) Details
8699394 Yamada K, Ono T, Nishioka H: Effect of NaN3 on oxygen-dependent lethality of UV-A in Escherichia coli mutants lacking active oxygen-defence and DNA-repair systems. Cancer Biochem Biophys. 1998 Jun;16(1-2):17-30.

Escherichia coli mutants which lack defence systems against such active oxygen forms as OxyR (delta oxyR), superoxide dismutase (SOD) (sodA and sodB) and catalase (katE and katG) are sensitive to UV-A lethality under aerobic conditions, whereas OxyR- and SOD-mutants have resistance under anaerobic conditions and in the presence of sodium azide (NaN3) during irradiation.
6(0,0,1,1) Details
10088602 Lundqvist-Gustafsson H, Bengtsson T: Activation of the granule pool of the NADPH oxidase accelerates apoptosis in human neutrophils. Am J Physiol. 1994 Apr;266(4 Pt 1):L397-404.

Exogenously added H2O2, together with the catalase blocker sodium azide, induced apoptosis to the same extent and with similar kinetics as PMA and ionomycin.
6(0,0,1,1) Details
10227157 Rafii F, Lunsford P, Hehman G, Cerniglia CE: Detection and purification of a catalase-peroxidase from Mycobacterium sp. J Neural Transm Suppl. 1994;41:35-9.

The enzyme was inhibited by sodium azide, glutathione, 2-mercaptoethanol, and isoniazid, but not by isonicotinic acid.
6(0,0,0,6) Details
9026352 Afonso SG, Polo CF, Enriquez de Salamanca R, Batlle A: Mechanistic studies on uroporphyrin I-induced photoinactivation of some heme-enzymes. Int J Biochem Cell Biol. 1996 Apr;28(4):415-20.

The presence of sodium azide, histidine or superoxide dismutase did not protect the enzymes against the effects of uroporphyrin I.
In the presence of either catalase or GSH, the enzyme photoinactivation was lower.
1(0,0,0,1) Details
15563529 Swafford AN Jr, Bratz IN, Knudson JD, Rogers PA, Timmerman JM, Tune JD, Dick GM: C-reactive protein does not relax vascular smooth muscle: effects mediated by sodium azide in commercially available preparations. J Enzyme Inhib. 2001;16(2):165-75.

Inhibition of vascular smooth muscle catalase with 3-amino-1,2,4-triazole completely prevented the effects of NaN (3) and NaN (3)-containing CRP solutions.
1(0,0,0,1) Details
9029274 Leeder RG, Rafeiro E, Brien JF, Mandin CC, Massey TE: Evaluation of reactive oxygen species involvement in amiodarone pulmonary toxicity in vivo and in vitro. J Biochem. 1995 Apr;117(4):780-6.


Incubation of macrophages with AM (73 or 146 microM) for 1 hour, with or without the catalase inhibitor sodium azide (1 mM), did not result in DCF formation.
0(0,0,0,0) Details
8766249 Roland J, Soranzo L, Launay JM, Vargaftig B: [Demonstration of the immunoreactivity of polynuclear eosinophils for bombesin and substance P. Clin Chim Acta. 2003 May;331(1-2):103-10.


Eosinophil peroxidases (catalases) should not affect the immunocytochemical reaction, since heating during a paraplast embedding and sodium-azide in electron microscopy procedure destroyed these enzymes.
0(0,0,0,0) Details
8929553 Bednar MM, Balazy M, Murphy M, Booth C, Fuller SP, Barton A, Bingham J, Golding L, Gross CE: Peroxynitrite augments fMLP-stimulated chemiluminescence by neutrophils in human whole blood. J Leukoc Biol. 1996 Nov;60(5):619-24.


Both sodium azide and taurine significantly inhibited LDCL (93% inhibition with 100 microM azide, 52% inhibition with 10 mM taurine).
0(0,0,0,0) Details
7954331 Sahu SC, Gray GC: Kaempferol-induced nuclear DNA damage and lipid peroxidation. Pharmacol Toxicol. 1995 Jan;76(1):50-5.

The kaempferol induced lipid peroxidation was significantly stimulated by catalase and sodium azide in the presence of iron (III).
6(0,0,1,1) Details
16124792 Wilson B, Gude L, Fernandez MJ, Lorente A, Grant KB: Tunable DNA photocleavage by an acridine-imidazole conjugate. . Toxicol Lett. 2007 Mar 30;169(3):253-8. Epub 2007 Feb 16.

Sodium azide, sodium benzoate, superoxide dismutase, and catalase indicate the involvement of type I and II photochemical processes in the metal-assisted DNA photocleavage reactions.
6(0,0,1,1) Details
7541472 Horwitz LD, Leff JA: Catalase and hydrogen peroxide cytotoxicity in cultured cardiac myocytes. . Inorg Chem. 2005 Sep 5;44(18):6159-73.

Inactivation or inhibition of catalase with aminotriazole or sodium azide increased LDH release but did not cause earlier release.
6(0,0,0,6) Details
11248219 Miura T, Muraoka S, Fujimoto Y: Inactivation of creatine kinase during the interaction of indomethacin with horseradish peroxidase and hydrogen peroxide: involvement of indomethacin radicals. Chem Biol Interact. 2001 Mar 14;134(1):13-25.

Adding catalase strongly inhibited the production of yellow substance.
Sodium azide also blocked the formation of yellow substance and the inactivation of CK.
1(0,0,0,1) Details
14687762 Abdel-Naim AB, Mohamadin AM: Myeloperoxidase-catalyzed oxidation of chloroacetonitrile to cyanide. . Toxicol Lett. 2004 Feb 2;146(3):249-57.

Addition of the MPO inhibitors; sodium azide (NaN3), 4-amino benzoic acid hydrazine (ABAH) or indomethacin to the reaction mixtures resulted in a significant decrease in the rate of CAN oxidation.
Inclusion of the antioxidant enzyme catalase (CAT) in the incubation mixtures resulted in a significant decrease in the rate of CAN oxidation and CN- formation.
1(0,0,0,1) Details
9061952 Bestwick CS, Brown IR, Bennett MH, Mansfield JW: Localization of hydrogen peroxide accumulation during the hypersensitive reaction of lettuce cells to Pseudomonas syringae pv phaseolicola. J Biochem Toxicol. 1996;11(3):147-60.


H2O2 production was reduced more by the inhibition of plant peroxidases (with potassium cyanide and sodium azide) than by inhibition of neutrophil-like NADPH oxidase (with diphenylene iodonium chloride).
0(0,0,0,0) Details
10491304 Osada M, Ogura Y, Yasui H, Sakurai H: Involvement of singlet oxygen in cytochrome P450-dependent substrate oxidations. Carcinogenesis. 1995 Apr;16(4):837-40.


The addition of beta-carotene, a quencher of singlet oxygen species ((1) O (2)), suppressed the aniline hydroxylation, while the addition of sodium azide (NaN (3)) ((1) O (2) quencher) enhanced the reaction.
0(0,0,0,0) Details
19199143 Szeto YT, Sok Wa Leong K, Keong Lam K, Min Min Hong C, Kai Mui Lee D, Teng Fun Chan Y, Benzie IF: Effects of incense smoke on human lymphocyte DNA. Am J Physiol Heart Circ Physiol. 2005 Apr;288(4):H1786-95. Epub 2004 Nov 24.

Catalase (CAT), sodium azide, and superoxide dismutase (SOD) were co-incubated with extract, which exerted significant DNA damaging effects.
6(0,0,1,1) Details
15386798 Zhu D, Xing D, Wei Y, Li X, Gao B: Evaluation of the degree of medical radiation damage with a highly sensitive chemiluminescence method. Carcinogenesis. 1996 Aug;17(8):1747-50.

In addition, the effects of catalase, Cu-Zn superoxide dismutase (SOD), mannitol, sodium azide (NaN (3)), and D (2) O on MCLA-dependent CL of lymphocytes are discussed.
6(0,0,1,1) Details
7828218 Li Y, Kuppusamy P, Zweier JL, Trush MA: ESR evidence for the generation of reactive oxygen species from the copper-mediated oxidation of the benzene metabolite, hydroquinone: role in DNA damage. Chem Biol Interact. 1995 Feb;94(2):101-20.


The presence of catalase also prevented the DNA damage.
1(0,0,0,1) Details
8023707 Arnhold J, Sonntag K, Sauer H, Hantzschel H, Arnold K: Increased native chemiluminescence in granulocytes isolated from synovial fluid and peripheral blood of patients with rheumatoid arthritis. J Mol Cell Cardiol. 1995 Mar;27(3):909-15.

Sodium azide strongly inhibited both kinds of luminescence.
A strong inhibition of the Type II native chemiluminescence was caused by desferal, catalase, thiourea, and glutathione.
1(0,0,0,1) Details
9260155 Sorg O, Horn TF, Yu N, Gruol DL, Bloom FE: Inhibition of astrocyte glutamate uptake by reactive oxygen species: role of antioxidant enzymes. Alcohol. 2007 Nov;41(7):525-34.


The inhibitory effect of hydrogen peroxide on glutamate uptake was not altered by the inhibition of glutathione peroxidase, whereas the inhibition of catalase by sodium azide clearly potentiated this effect.
0(0,0,0,0) Details
19170773 Nascimento H, Belo L, Fernandes J, Rocha S, Quintanilha A, Santos-Silva A: In vitro studies with 'acatalasemic-like' erythrocytes and hydrogen peroxide: attention to the formation of lysis resistant erythrocytes. Int J Lab Hematol. 2009 Jan 17.

Summary Hemolysis assays, using hydrogen peroxide as an oxidant injury agent and sodium azide as a catalase inhibitor, were performed to evaluate how assay conditions affect the development of lysis resistant erythrocytes.
31(0,1,1,1) Details
9300140 Sarkar B, Das U, Bhattacharyya S, Bose SK: Studies on the aerobic photooxidation of cysteine using riboflavin as a sensitizer: evidence for the photogeneration of a superoxide anion and hydrogen peroxide. Am J Physiol Heart Circ Physiol. 2009 Sep;297(3):H930-48. Epub 2009 Jun 19.

The effects of various scavengers, such as superoxide dismutase, catalase, mannitol, sodium azide and potassium ferrocyanide (an electron donor), on the photooxidation were determined.
6(0,0,1,1) Details
9358240 Zhang X, Rosenstein BS, Wang Y, Lebwohl M, Wei H: Identification of possible reactive oxygen species involved in ultraviolet radiation-induced oxidative DNA damage. Free Radic Biol Med. 1994 Dec;17(6):557-67.

Sodium azide, a singlet oxygen (1O2) scavenger though its quenching effect on HO. was also reported, inhibited 8-oxodGuo production in calf thymus DNA exposed to UVA, UVB, or UVC in a concentration-dependent fashion with maximal quenching effect of over 90% at a concentration of 10 mM.
Catalase, at a concentration of 50 U/ml, reduced the yields of UVA- and UVB-induced 8-oxodGuo formation by approximately 50%, but had little effect on UVC-induced 8-oxodGuo production.
1(0,0,0,1) Details
18722362 Prigol M, Wilhelm EA, Schneider CC, Nogueira CW: Protective effect of unsymmetrical dichalcogenide, a novel antioxidant agent, in vitro and an in vivo model of brain oxidative damage. Biochim Biophys Acta. 2004 Apr 5;1688(3):257-64.

The levels of lipid peroxidation and the activity of catalase, glutathione peroxidase (GPx), glutathione S-transferase (GST) and glutathione reductase (GR) were carried out in brain homogenates of SNP-injected mice.
Unsymmetrical dichalcogenides (1-3) were tested against lipid peroxidation induced by sodium nitroprusside (SNP) or malonate, and reactive species (RS) production induced by sodium azide in rat brain homogenates.
1(0,0,0,1) Details
15349518 Kartvelishvili T, Abuladze M, Asatiani N, Akhvlediani J, Kiziria E, Asanishvili L, Lejava L, Holman HY, Sapojnikova N: Estimation of the cellular antioxidant response to chromium action using ESR method. Invest Ophthalmol Vis Sci. 1996 Jul;37(8):1549-56.

The crude cell extracts of the cells grown in the presence of 2 microM (nontoxic) and 20 microM (toxic) chromium (VI) concentrations were tested in the model Fenton system with and without catalase-inhibitor sodium azide.
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8892520 Salmela KS, Kaihovaara P, Salaspuro M, Roine RP: Role of catalase in rat gastric mucosal ethanol metabolism in vitro. Lasers Surg Med. 1998;22(4):212-8.

Catalase inhibitors sodium azide (SA) and 3-amino-1,2,4-triazole (3-AT) had little effect on ADH activity but markedly decreased catalase activity and acetaldehyde formation (1 mM of SA to 56 +/- 13% of control, 5 mM of 3-AT to 67 +/- 3% of control; mean +/- SE). 4-Methylpyrazole decreased ADH activity significantly, but did not affect acetaldehyde formation.
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9300794 Masuoka N, Wakimoto M, Ohta J, Ishii K, Nakano T: Characterization of hydrogen peroxide removal activities in mouse hemolysates: catalase activity and hydrogen peroxide removal activity by hemoglobin. Biochim Biophys Acta. 1997 Aug 22;1361(2):131-7.

The removal activity deactivated at a higher temperature remained after the addition of sodium azide, and the 50% inactivation was observed at 63.5 +/- 1.4 degrees C.
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10986644 Ardelli BF, Witt JD, Woo PT: Identification of glycosomes and metabolic end products in pathogenic and nonpathogenic strains of Cryptobia salmositica (Kinetoplastida: Bodonidae). Arch Biochem Biophys. 1994 Apr;310(1):210-7.


The glycolytic enzymes hexokinase, fructose-1,6-biphosphate aldolase, triosephosphate isomerase, glucosephosphate isomerase and glyceraldehyde-3-phosphate-dehydrogenase and the peroxisomal enzyme catalase were associated with a microbody that had a buoyant density in sucrose of 1.21 g cm-3.
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15962938 Park JH, Gopishetty S, Szewczuk LM, Troxel AB, Harvey RG, Penning TM: Formation of 8-oxo-7,8-dihydro-2'-deoxyguanosine (8-oxo-dGuo) by PAH o-quinones: involvement of reactive oxygen species and copper (II)/copper (I) redox cycling. Chem Res Toxicol. 2005 Jun;18(6):1026-37.

It was completely or partially inhibited when catalase, tiron, or a Cu (I) specific chelator, bathocuproine, was added, indicating the requirement for H (2) O (2), O (2)(-), and Cu (I), respectively.
Sodium azide, which can act as both a hydroxyl radical and a (1) O (2) scavenger, abolished the formation of 8-oxo-dGuo.
1(0,0,0,1) Details
15708802 Dhar S, Nethaji M, Chakravarty AR: Effect of charge transfer bands on the photo-induced DNA cleavage activity of [1-(2-thiazolylazo)-2-naphtholato] copper (II) complexes. J Inorg Biochem. 2005 Mar;99(3):805-12.

The cleavage reactions involve the formation reactive hydroxyl species as significant inhibition in the presence of dimethyl sulfoxide (DMSO) and catalase is observed.
There is no apparent inhibition in cleavage in the presence of singlet oxygen quenchers like sodium azide.
1(0,0,0,1) Details
9464485 Okubo T, Nagai F, Ushiyama K, Yokoyama Y, Ozawa S, Kano K, Tomita S, Kubo H, Kano I: DNA cleavage and 8-hydroxydeoxyguanosine formation caused by tamoxifen derivatives in vitro. Alcohol Clin Exp Res. 1997 Sep;21(6):1063-72.

The DNA cleavage by N-desmethyltamoxifen was inhibited by the addition of EDTA, mannitol, sodium azide, methionine, catalase and superoxide dismutase.
31(0,1,1,1) Details
11506893 Kim RH, Kwon OJ, Park JW: Ceruloplasmin enhances DNA damage induced by cysteine/iron in vitro. Eur J Biochem. 2000 Sep;267(17):5585-92.

The capacity of Cp to enhance oxidative damage to DNA was inhibited by hydroxyl radical scavengers such as sodium azide and mannitol, a metal chelator, diethylenetriaminepentaacetic acid, a spin-trapping agent, 5,5-dimethyl-1-pyrroline N-oxide (DMPO) and catalase.
31(0,1,1,1) Details
8643080 Li Y, Kuppusamy P, Zweir JL, Trush MA: Role of Cu/Zn-superoxide dismutase in xenobiotic activation. J Hypertens. 1998 Mar;16(3):291-303.

Incubation of the plasmid DNA with the HQ/Cu/Zn-SOD system resulted in the induction of single- as well as double-strand breaks, which could be inhibited by catalase and the Cu (I) chelators, bathocuproinedisulfonic acid (BCS) and GSH.
Similar to the HQ/Cu (II) and H202/Cu (II) systems, the DNA strand breaks mediated by HQ/Cu/Zn-SOD could not be effectively inhibited by the hydroxyl radical scavengers, including dimethylsulfoxide, mannitol, and 5,5-dimethyl-1-pyrroline N-oxide, but could be protected by sodium azide.
4(0,0,0,4) Details
11411221 Chen J, Zhu TB, Zhang YF, Yang YL, Jiao RS: [Enzymatic conversion of cephalosporin C to glutaryl-7-aminocephalosporanic acid using whole cells of the yeast Trigonopsis variabilis FA10]. Sheng Wu Gong Cheng Xue Bao. 2001 Mar;17(2):150-4.


It was found that the bioconversion of CPC to GL-7ACA was interfered by the catalase activity presented in the cells that hydrolyzed the hydrogen peroxide and resulted in the accumulation of alpha-keto-adipyl-7-ACA (AKA-7ACA) and decrease of GL-7ACA yield. the methods to overcome this problem including the addition of extra H2O2 and use of catalase inhibitor, NaN3, were developed and the rate of GL-7ACA from CPC were 73% and 70.1%, respectively.
3(0,0,0,3) Details
19542485 Mink SN, Jacobs H, Cheng ZQ, Kasian K, Santos-Martinez LE, Light RB: Lysozyme, a mediator of sepsis that intrinsically generates hydrogen peroxide to cause cardiovascular dysfunction. J Appl Toxicol. 2004 Mar-Apr;24(2):99-106.

We found that Lzm-S could generate H (2) O (2) and, furthermore, that this generation could be attenuated by the singlet oxygen quencher sodium azide.
In a canine ventricular trabecular preparation, we found that the peroxidizing agent Aspergillus niger catalase, that would breakdown H (2) O (2), prevented Lzm-S- induced decrease in contraction.
1(0,0,0,1) Details
12184785 Oikawa S, Hiraku Y, Fujiwara T, Saito I, Kawanishi S: Site-specific hydroxylation at polyguanosine in double-stranded DNA by nickel (II) in the presence of SH compounds: comparison with singlet oxygen-induced DNA damage. Mol Pharmacol. 1996 Mar;49(3):412-21.

SOD and catalase inhibited the DNA damage, suggesting that DNA damage involved superoxide anion and hydrogen peroxide.
Sodium azide, a potent and relatively specific scavenger of (1) O (2), inhibited DNA damage by Ni (II) in the presence of DTT, whereas the sequence specificity of DNA damage was different from that obtained by (1) O (2) generating agent.
1(0,0,0,1) Details
8747893 Salman-Tabcheh S, Guerin MC, Torreilles J: Potential role of the peroxidase-dependent metabolism of serotonin in lowering the polymorphonuclear leukocyte bactericidal function. Free Radic Res. 1996 Jan;24(1):61-8.

The addition of catalase or sodium azide substantially reduced this binding.
31(0,1,1,1) Details
9343371 Qiu XB, Cadenas E: The role of NAD (P) H:quinone oxidoreductase in quinone-mediated p21 induction in human colon carcinoma cells. Arch Biochem Biophys. 1997 Oct 15;346(2):241-51.

At variance with HT29 cells, H2O2 formation by BE cells was insensitive to the catalase inhibitor sodium azide.
31(0,1,1,1) Details
8302290 Chatterjee U, Sanwal GG: Purification and characterization of catalase from goat (Capra capra) lung. Cancer Lett. 1998 Mar 13;125(1-2):117-21.

Tryptophan, indole acetic acid, cysteine, formaldehyde and sodium azide inhibited the enzyme non-competitively with Ki values of 1.5, 1.6, 6.7, 0.55 and 0.0017 mM, respectively.
3(0,0,0,3) Details
8918957 Roberts B, Hirst R: Identification and characterisation of a superoxide dismutase and catalase from Mycobacterium ulcerans. Dis Aquat Organ. 2000 Aug 10;42(1):41-51.

3(0,0,0,3) Details
9390169 Reinke LA, Moore DR, McCay PB: Mechanisms for metabolism of ethanol to 1-hydroxyethyl radicals in rat liver microsomes. Arch Biochem Biophys. 1997 Dec 1;348(1):9-14.


The variables tested include addition of azide, catalase, superoxide dismutase, and deferoxamine, or use of phosphate or Tris buffers.
2(0,0,0,2) Details
10716039 Jordan CG, Brown K, Beedham C, Brown JE: Effect of inhibitors on the biotransformation of tamoxifen by female rat and mouse liver slices and homogenates. J Biolumin Chemilumin. 1995 Jul-Aug;10(4):229-37.

When rat liver homogenates was incubated with superoxide dismutase (SOD) and catalase, it was observed that the N-desmethyl metabolite disappeared completely at 60 min and the N-oxide and 4-hydroxy metabolites were completely inhibited.
Female rat liver slices and homogenates were incubated with the following inhibitors (1 mM): cimetidine, ascorbate, sodium azide and reduced glutathione.
2(0,0,0,2) Details
10193578 Gutierrez-Correa J, Stoppani AO: Inactivation of myocardial dihydrolipoamide dehydrogenase by myeloperoxidase systems: effect of halides, nitrite and thiol compounds. Free Radic Res. 1999 Feb;30(2):105-17.

The effect of the MPO/H2O2/NaNO2 system was prevented by MPO inhibitors (sodium azide, isoniazid, salicylhydroxamic acid) and also by L-cysteine, L-methionine, L-tryptophan, L-tyrosine, L-histidine and reduced glutathione.
LADH inactivation by the MPO/NADH/halide systems was prevented by catalase and enhanced by superoxide dismutase, in close agreement with H2O2 production by the LADH/NADH system.
1(0,0,0,1) Details
8161207 Partridge RS, Monroe SM, Parks JK, Johnson K, Parker WD Jr, Eaton GR, Eaton SS: Spin trapping of azidyl and hydroxyl radicals in azide-inhibited rat brain submitochondrial particles. Luminescence. 2004 Sep-Oct;19(5):278-82.


The concentrations of both DMPO/.OH and DMPO/.N3 were decreased by addition of catalase to the smps, which indicates that H2O2 is involved in radical production.
1(0,0,0,1) Details
9603282 Grossman N, Schneid N, Reuveni H, Halevy S, Lubart R: 780 nm low power diode laser irradiation stimulates proliferation of keratinocyte cultures: involvement of reactive oxygen species. J Cell Biochem. 2001 Aug 21-Sep 5;83(3):473-83.

Added enzymatic antioxidants, superoxide dismutase or catalase, scavenging superoxide anions and H2O2, suppressed this enhanced proliferation.
Added scavengers (alpha-tocopherol acetate, scavenging lipid peroxidation, or sodium azide, histidine, mannitol, scavenging singlet oxygen, superoxide anions, and hydroxyl radicals, respectively), or N-acetyl cysteine, the thiol-reducing agent, suppressed the response, but to different extents.
1(0,0,0,1) Details
10393704 Anderson MM, Requena JR, Crowley JR, Thorpe SR, Heinecke JW: The myeloperoxidase system of human phagocytes generates Nepsilon-(carboxymethyl) lysine on proteins: a mechanism for producing advanced glycation end products at sites of inflammation. J Clin Invest. 1999 Jul;104(1):103-13.


CML production by neutrophils was inhibited by the H2O2 scavenger catalase and the heme poison azide, implicating myeloperoxidase in the cell-mediated reaction.
1(0,0,0,1) Details
16568613 Iakovenko IN, Zhirnov VV: [Sodium azide as indirect nitric oxide donor: researches on the rat aorta isolated segments]. Alcohol Clin Exp Res. 1996 Sep;20(6):1011-5.

It was found that H2O2 injection to physiological solution containing NaN3 and horseradish peroxidase or catalase lead to NO2- accumulation in it, which was blocked by NaCN.
1(0,0,0,1) Details
17900002 Okai Y, Sato EF, Higashi-Okai K, Inoue M: Potentiating effect of an endocrine disruptor, paranonylphenol, on the generation of reactive oxygen species (ROS) in human venous blood -- association with the activation of signal transduction pathway. J UOEH. 2007 Sep 1;29(3):221-33.

ROS-scavenging enzymes such as catalase and superoxide dismutase, and the lipophilic antioxidative agents, alpha-tocopherol and beta-carotene, showed preventive effects on NP-induced ROS generation.
An NADPH-dependent oxidase inhibitor, diphenyl iodonium chloride (DPI), and a myeloperoxidase inhibitor, sodium azide (NaN3), showed remarkable inhibitory effects on ROS generation induced by NP, but an inhibitor against mitochondrial respiratory function, potassium cyanide (KCN), did not exhibit a significant effect.
1(0,0,0,1) Details
17350187 Zuo GC, Yang JY, Hao Y, Dong YX, Wu CF: Ethanol and acetaldehyde induce similar changes in extracellular levels of glutamate, taurine and GABA in rat anterior cingulate cortex. Int J Lab Hematol. 2008 Dec 4.

Interestingly, similar changes of these amino acids were induced by ethanol (EtOH, 3 g/kg, i.p.) when sodium azide (NaN3, 10 mg/kg, i.p.), a catalase inhibitor that can reduce brain ethanol metabolism, was used simultaneously.
31(0,1,1,1) Details
12123818 Wang J, Xing D, He Y, Hu X: Experimental study on photodynamic diagnosis of cancer mediated by chemiluminescence probe. J Radiat Res. 1996 Mar;37(1):29-37.

The chemiluminescence was markedly inhibited by the addition of 10 mmol/l sodium azide (NaN (3)) to the model solution and minor effects were observed at the addition of 10 micromol/l superoxide dismutase, 20 mmol/l mannitol and 100 microg/ml catalase, respectively, thus indicating that (1) O (2) generation from photosensitization reaction mainly results in light emission.
31(0,1,1,1) Details
9309319 Hamby-Mason R, Chen JJ, Schenker S, Perez A, Henderson GI: Catalase mediates acetaldehyde formation from ethanol in fetal and neonatal rat brain. Biochem Biophys Res Commun. 1994 Apr 29;200(2):966-72.

When incubated with CAT inhibitors (sodium azide or 3-aminotriazole), AcHO formation was blocked, whereas neither the alcohol dehydrogenase inhibitor, 4-methylpyrazole, nor P-450 inhibitors decreased AcHO production.
2(0,0,0,2) Details
9718094 VanUffelen BE, Van der Zee J, de Koster BM, VanSteveninck J, Elferink JG: Sodium azide enhances neutrophil migration and exocytosis: involvement of nitric oxide, cyclic GMP and calcium. Free Radic Res. 2001 Dec;35(6):735-47.

Azide can be oxidized by catalase and myeloperoxidase in the presence of H2O2, resulting in the generation of nitric oxide (NO).
2(0,0,0,2) Details
9254898 Maramag C, Menon M, Balaji KC, Reddy PG, Laxmanan S: Effect of vitamin C on prostate cancer cells in vitro: effect on cell number, viability, and DNA synthesis. Mol Med. 1997 Jul;3(7):431-40.

However, that singlet oxygen scavengers such as sodium azide and hydroquinone and hydroxyl radical scavengers such as D-mannitol and DL-alpha-tocopherol did not counteract the effects of ascorbic acid on thymidine incorporation suggests that vitamin C-induced changes do not occur through the generation of these ROS.
Vitamin C induced these changes through the production of hydrogen peroxide; addition of catalase (100-300 units/ml), an enzyme that degrades hydrogen peroxide, inhibited the effects of ascorbic acid.
1(0,0,0,1) Details
15064160 Okai Y, Sato EF, Higashi-Okai K, Inoue M: Enhancing effect of the endocrine disruptor para-nonylphenol on the generation of reactive oxygen species in human blood neutrophils. J Biol Chem. 2000 Jun 23;275(25):19241-9.

Furthermore, ROS-scavenging enzymes such as catalase and superoxide dismutase and antioxidative agents alpha-tocopherol and beta-carotene showed strong preventive effects on NP-induced ROS generation.
Reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent oxidase inhibitor, diphenyl iodonium chloride and the myeloperoxidase inhibitor sodium azide (NaN3) showed remarkable inhibitory effects on ROS generation induced by NP, but an inhibitor against mitochondrial respiratory function, potassium cyanide (KCN), did not exhibit significant effect.
1(0,0,0,1) Details
9801073 Lacy F, Gough DA, Schmid-Schonbein GW: Role of xanthine oxidase in hydrogen peroxide production. . J Nutr Biochem. 2001 Sep;12(9):505-511.

In the presence of sodium azide, an inhibitor of catalase, peroxide production was measured in plasma after adding xanthine or xanthine oxidase and the results were similar to those obtained in buffered saline.
In the presence of sodium azide, an inhibitor of catalase, peroxide production was measured in plasma after adding xanthine or xanthine oxidase and the results were similar to those obtained in buffered saline.
1(0,0,0,1) Details
17590992 Jamal M, Ameno K, Ikuo U, Kumihashi M, Wang W, Ijiri I: Ethanol and acetaldehyde: in vivo quantitation and effects on cholinergic function in rat brain. Novartis Found Symp. 2007;285:137-41; discussion 141-4

The study suggested that catalase made a significant contribution to acetaldehyde formation in the rat brain, and that EtOH and acetaldehyde decreased ChAT expression at 40 and 240 min after EtOH dosing.
The results showed that acetaldehyde was present in the cyanamide (CY) + EtOH, CY + 4-methylpyrazole (4-MP) + EtOH and CY + sodium azide + EtOH groups.
1(0,0,0,1) Details
15763969 Shi M, Xu B, Azakami K, Morikawa T, Watanabe K, Morimoto K, Komatsu M, Aoyama K, Takeuchi T: Dual role of vitamin C in an oxygen-sensitive system: discrepancy between DNA damage and cell death. Free Radic Res. 2005 Feb;39(2):213-20.

In the presence of vitamin C, the 8-hydroxydeoxyguanosine (8OHdG) formation induced by oxygen exposure was enhanced, probably due to the action of vitamin C on hydrogen peroxide generated during oxygen exposure: while catalase almost completely suppressed the enhancing effect of vitamin C, 8OHdG formation induced by hydrogen peroxide was enhanced by vitamin C.
Sodium azide showed similar effects to vitamin C, thus the antioxidant action of vitamin C may be due to its quenching of the singlet oxygen generated in this system.
1(0,0,0,1) Details
8565117 Tsou TC, Chen CL, Liu TY, Yang JL: Induction of 8-hydroxydeoxyguanosine in DNA by chromium (III) plus hydrogen peroxide and its prevention by scavengers. Carcinogenesis. 1996 Jan;17(1):103-8.

Scavengers of reactive oxygen species markedly inhibited the formation of 8-OHdG by CrCl3 plus H2O2; the inhibition effect was sodium azide > D-mannitol > Tris-HCl at an equal concentration.
Moreover, an addition of catalase (2.2 U/ml) to the reaction mixture completely inhibited the formation of 8-OHdG by CrCl3/H2O2, whereas only 22% of that formation was inhibited by superoxide dismutase (11 U/ml).
1(0,0,0,1) Details
9360968 Yu R, Tan TH, Kong AN: Butylated hydroxyanisole and its metabolite tert-butylhydroquinone differentially regulate mitogen-activated protein kinases. Neurotoxicology. 2007 Nov;28(6):1245-8. Epub 2007 May 13.


Furthermore, BHA and tBHQ activation of ERK2 was strongly inhibited by ascorbic acid and a peroxidase inhibitor, sodium azide, suggesting the potential role of phenoxyl radicals and/or their derivatives.
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8016214 Kato Y, Uchida K, Kawakishi S: Aggregation of collagen exposed to UVA in the presence of riboflavin: a plausible role of tyrosine modification. Invest Ophthalmol Vis Sci. 2000 Sep;41(10):3176-82.


Sodium azide or 1,4-diazabicyclo (2,2,2) octane, which are known to be singlet oxygen quenchers, and catalase could not inhibit the modification.
0(0,0,0,0) Details
10579466 Orie NN, Zidek W, Tepel M: Tyrosine and calcium/calmodulin kinases are common signaling components in the generation of reactive oxygen species in human lymphocytes. Histochem J. 2001 May;33(5):273-81.


These increases were significantly inhibited by catalase, sodium azide, and dimethylsulfoxide but not by superoxide dismutase, suggesting that the ROS apparently included hydrogen peroxide, singlet oxygen and hydroxyl ion but not superoxide anion.
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8031139 Park JW, Floyd RA: Generation of strand breaks and formation of 8-hydroxy-2'-deoxyguanosine in DNA by a Thiol/Fe3+/O2-catalyzed oxidation system. Acta Biochim Pol. 2006;53(3):577-84. Epub 2006 Sep 4.


Sodium azide and mannitol as well as a metal chelator, diethylenetriaminepentaactic acid, decreased strand breaks and 8-OH-dG formation in DNA.
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