| Literature DB >> 235764 |
Abstract
Glutathione reductase from rabbit erythrocytes was pruified to homogeneity and found to be a monomer with a mol wt of 60,000. Both NADPH and HADH were capable of acting as cofactors for the reduction of GSSG and the following kinetic values were obtained: Km, GSSG = 120 muM; Km, NADPH = 37 muM; Vmax = 23 mumoles NADPH/min/mg protein, Km, NADH = 420 muM; Vmax = 3 mumoles NADH/min/mg protein. Rabbit erythrocyte GR exhibited substrate inhibition, and was susceptible to inhibition by p-hydroxymercuribenzoate under certain conditions.Entities:
Mesh：
Substances：
Year: 1975 PMID： 235764 DOI： 10.3181/00379727-148-38548
Source DB: PubMed Journal: Proc Soc Exp Biol Med ISSN： 0037-9727