Jody M. Prescott

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Apoenzyme prepared by removal of the 2 mol of Zn2+/mol from Aeromonas aminopeptidase is inactive. Addition of Zn2+ reactivates it completely, and reconstitution with Co2+, Ni2+, or Cu2+ results in a 5.0-, 9.8-, and 10-fold more active enzyme than native aminopeptidase, respectively. Equilibrium dialysis and spectral titration experiments with Co2+ confirm(More)
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;(More)
Full substitution of Cu(II) or Ni(II) for the two g-atom zinc in Aeromonas aminopeptidase hyperactivates the enzyme 6.5 and 25 fold respectively. Even greater enhancements of activity can be achieved with mixed metal substitutions. Thus, apoenzyme reactivated by first adding one g-atom zinc followed by one g-atom of either Cu(II) or Ni(II) is 15 and 22(More)