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The inactivation of rhodanese by nitrite and inhibition by other anions in vitro

✍ Scribed by Alexander, Keith ;Procell, Lawrence R. ;Kirby, Stephen D. ;Baskin, Steven I.


Publisher
John Wiley and Sons
Year
1989
Tongue
English
Weight
436 KB
Volume
4
Category
Article
ISSN
0887-2082

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The rat liver rhodanese (thiosulphate: cyanide sulfurtransferase EC 2.6.1.1) has been immobilized on polyacrylamide gels. The immobilized enzyme had a pH optimum of 7.4 and Km values of 3.25 mM and 1.12 mM for S20g-and KCN, respectively. The enzyme was competitively inhibited by NaNO, and CH,COONa a

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The uncoupling agent, 2,4-dinitrophenol, inhibits the reduction of nitrite by the green alga Ankistrodesmus braunii but does not appear to prevent the reduction of nitrate (K~SSLm~, 1955;1959). This latter conclusion was based on the observation that nitrite accumulates in the medium when the alga i