Isolation and some characteristics of glutathione reductase from rabbit erythrocytes (38548).
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.
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000201:enzymology*; D005260:Female; D005978:Glutathione; D005980:Glutathione Reductase / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D006902:Hydroxymercuribenzoates; D007700:Kinetics; D008297:Male; D008970:Molecular Weight; D009249:NADP; D011817:Rabbits / Q000097:blood*; D012965:Sodium Chloride; D014508:Urea
D006902:Hydroxymercuribenzoates; D012965:Sodium Chloride; D009249:NADP; D014508:Urea; D005980:Glutathione Reductase; D005978:Glutathione