Name | DTNB |
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Synonyms | Beta dystrobrevin; DTN B; DTNB; Dystrobrevin beta; Dystrobrevin betas |
Name | sodium arsenite |
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CAS | sodium arsenenite |
PubMed | Abstract | RScore(About this table) | |
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1575728 | Lenartowicz E: Ca (2+)-sensitive reduction of 5,5'-dithiobis-(2-nitrobenzoic acid) by rat liver mitochondria. Biochem Biophys Res Commun. 1992 Apr 30;184(2):1088-93. After lysis of mitochondria the reduction of DTNB required the addition of and EGTA and was inhibited by 1 mM sodium arsenite. |
84(1,1,1,4) | Details |
1125817 | Lin WS, Armstrong DA, Gaucher GM: Formation and repair of papain sulfenic acid. Can J Biochem. 1975 Mar;53(3):298-307. These discrepancies resulted from the reaction of inactive papain with either the thiol anion product of the DTNB reaction, or with the pHMB reagent itself. Sodium arsenite, which is capable ofreducing sulfenic acids but not disulfide bonds, readily repaired peroxide-inactivated papain. |
2(0,0,0,2) | Details |
1181010 | Symes AL, Sourkes TL: Essential sulfhydryl groups of rat liver monoamine oxidase. . Can J Biochem. 1975 Aug;53(8):910-3. Sodium nitroprusside and 5,5'-dithiobis (2-nitrobenzoic acid) (DTNB) inhibited the enzyme, apparently reversibly, while sodium arsenite was not inhibitory. The average number of sulfhydryl groups per mole of enzyme, determined by reaction with DTNB, increased from 3.6 +/- 0.2 freely reacting sulfhydryl groups (n = 4) to 18.4 to total sulfhydryl groups (n = 2) on denaturation with 8 M urea. |
1(0,0,0,1) | Details |
7925850 | Gargari ML, Bansal RC, Singh K, Mahmood A: Inhibition of transport in human erythrocytes by 2,3-dioxoindole (isatin). Experientia. 1994 Sep 15;50(9):833-6. The observed inhibition of sugar transport by isatin was not mediated through membrane -SH groups accessible to iodoacetate, iodoacetamide, DTNB, DNP or sodium arsenite. |
0(0,0,0,0) | Details |
9027754 | Brown DM, Upcroft JA, Upcroft P: A thioredoxin reductase-class of disulphide reductase in the protozoan parasite Giardia duodenalis. Mol Biochem Parasitol. 1996 Dec 20;83(2):211-20. The sulphydryl-active compounds, N-ethylmaleimide, sodium arsenite and Zn2+ ions, strongly inhibited the enzyme suggesting that a thiol component forms part of the active site. |
0(0,0,0,0) | Details |