Protein Information

Name DTNB
Synonyms Beta dystrobrevin; DTN B; DTNB; Dystrobrevin beta; Dystrobrevin betas

Compound Information

Name sodium arsenite
CAS sodium arsenenite

Reference List

PubMed Abstract RScore(About this table)
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 NADPH 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 glucose 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