| Name | protein as |
|---|---|
| Synonyms | A1 activator; PSAP; Protein C; CSAct; Cerebroside sulfatase activator; Cerebroside sulfate activator; Co beta glucosidase; Component C… |
| Name | sodium azide |
|---|---|
| CAS | sodium azide |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 8521866 | Yang S, Enfors SO: The influence of energy sources on the proteolysis of a recombinant staphylococcal protein A in Escherichia coli. Eur J Biochem. 1995 Nov 1;233(3):969-75. The respiration inhibitor sodium azide completely inhibited the degradation of protein A in -free salt medium but had almost no effect in the presence of |
5(0,0,0,5) | Details |
| 7849984 | Shi JY, Goffe RA: Comprehensive study on binding capacity of human immunoglobulin G to Avid AL affinity gel. J Chromatogr A. 1994 Nov 25;686(1):61-71. Recombinant Protein A gel was used as a control. |
1(0,0,0,1) | Details |
| 16034640 | Baby SM, Roy A, Lahiri S: Role of mitochondria in the regulation of hypoxia-inducible factor-1alpha in the rat carotid body glomus cells. Histochem Cell Biol. 2005 Jul;124(1):69-76. Epub 2005 Jul 22. Hypoxia-inducible factor-1alpha (HIF-1alpha) protein, a heterodimeric transcription factor that regulates transcriptional activation of several genes, is involved in adaptive responses to hypoxia. To test this hypothesis in the CB glomus cells, we studied the effect of mitochondrial electron transport chain (ETC) inhibitors: rotenone (complex I; 1 microM), (complex II; 0.5 M), antimycin A (complex III; 1 microg/ml), sodium azide (complex IV; 5 mM), and uncoupler of oxidative phosphorylation: carbonyl p-trifluoromethoxyphenylhydrazone (FCCP; 1 mM) on HIF-1alpha expression during normoxia and hypoxia. |
1(0,0,0,1) | Details |
| 15942677 | Doublier S, Musante L, Lupia E, Candiano G, Spatola T, Caridi G, Zennaro C, Carraro M, Ghiggeri GM, Camussi G: Direct effect of plasma permeability factors from patients with idiopatic FSGS on nephrin and podocin expression in human podocytes. Int J Mol Med. 2005 Jul;16(1):49-58. Purification procedure was based on protein A Sepharose chromatography and differential precipitation in ammonium sulphate. This effect was associated with cytoskeleton redistribution and inhibited by cytochalasin B and sodium azide. |
1(0,0,0,1) | Details |
| 7629156 | Berghofer J, Karnauchov I, Herrmann RG, Klosgen RB: Isolation and characterization of a cDNA encoding the SecA protein from spinach chloroplasts. J Biol Chem. 1995 Aug 4;270(31):18341-6. Comparably to E. coli, in which SecA activity can be inhibited by sodium azide, thylakoid translocation of a subset of lumenal proteins is sensitive to sodium azide in pea but not in spinach chloroplasts, suggesting that the latter contain an azide-resistant SecA variant. One of these routes is related to the prokaryotic Sec pathway, which mediates the secretion of particular proteins into the periplasmic space and involves the SecA protein as an essential component. |
1(0,0,0,1) | Details |
| 10327596 | Gollas-Galvan T, Hernandez-Lopez J, Vargas-Albores F: Prophenoloxidase from brown shrimp (Penaeus californiensis) hemocytes. Comp Biochem Physiol B Biochem Mol Biol. 1999 Jan;122(1):77-82. The isolated proPO is a 114-kDa monomeric protein as determined by SDS-PAGE. The PO reaction using as substrate, has an optimum pH of 8, and was poorly inhibited by sodium azide, thiourea and EDTA, but strongly inhibited by diethyl thiocarbamate. |
1(0,0,0,1) | Details |
| 19384921 | Roy S, Mason BD, Schoneich CS, Carpenter JF, Boone TC, Kerwin BA: Light-induced aggregation of type I soluble tumor necrosis factor receptor. J Pharm Sci. 2009 Sep;98(9):3182-99. Intermolecular disulfide formation was also directly correlated with the photoinduced unfolding of the protein as measured by changes in secondary structure by CD spectroscopy. |
1(0,0,0,1) | Details |
| 17646712 | Seo SN, Lee JH, Kim YM: Characterization of an iron- and manganese-containing superoxide dismutase from Methylobacillus sp. strain SK1 DSM 8269. Mol Cells. 2007 Jun 30;23(3):370-8. peroxide and sodium azide, but not was found to inhibit the purified enzyme. The final specific activity was 4,831 units per milligram protein as determined by an assay based on a 50% decrease in the rate of cytochrome c reduction. |
1(0,0,0,1) | Details |
| 8675397 | Giangiacomo A, Olesen PR, Ortwerth BJ: and oxidation by ultraviolet A-generated free radicals. Invest Ophthalmol Vis Sci. 1996 Jul;37(8):1549-56. The role of individual reactive species was determined by the protective effects of superoxide dismutase, catalase, and sodium azide. UVA irradiation with 2 mg/ml human lens protein as sensitizer oxidized 1 mM ASA after several hours but oxidized, at most, only 2 microM even after 8 hours of irradiation. |
1(0,0,0,1) | Details |
| 10328762 | Pai JJ, Kirkup MP, Frank EA, Pachter JA, Bryant RW: Compounds capable of generating singlet represent a source of artifactual data in scintillation proximity assays measuring phosphopeptide binding to SH2 domains. Anal Biochem. 1999 May 15;270(1):33-40. The SPA used an antibody to couple glutathione-S-transferase SH2 domain fusion proteins to scintillant beads coated with protein A. Their inhibitory activity was suppressed by the singlet scavengers sodium azide and |
1(0,0,0,1) | Details |
| 9509413 | An SS, Kim YM: Purification and characterization of a manganese-containing superoxide dismutase from a carboxydobacterium, Pseudomonas carboxydohydrogena. Mol Cells. 1997 Dec 31;7(6):730-7. Sodium azide, but not and peroxide, was found to inhibit the enzyme activity. The final specific activity was 2,396 units per mg protein as determined by an assay based on a 50% decrease in the rate of cytochrome c reduction. |
1(0,0,0,1) | Details |
| 9038303 | Brogden K, Clarke C: Increase of glycocalyx and altered lectin agglutination profiles of Pasteurella haemolytica A1 after incubation in bovine subcutaneous tissue chambers in vivo or in ruminant serum in vitro. Infect Immun. 1997 Mar;65(3):957-63. Agglutination profiles were then determined with 17 lectins in 10 mM HEPES-buffered saline (pH 8.4) with 0.1 mM CaCl2 and 0.08% sodium azide. |
0(0,0,0,0) | Details |