
pmid: 8660320
A GSH-dependent dehydroascorbate reductase (EC 1.8.5.1) was purified to homogeneity from human erythrocytes. The enzyme was a monomer of 32 kDa and was purified 133-fold from a crude DEAE-Sepharose fraction with a 25% yield. The reduced protein had a pI of 5.1 as judged by isoelectric focusing. Kinetic analysis gave a Kcat of 316 min-1, a Km of 0.21 mM for DHA with a Kcat/Km of 2.47 x 10(4) M-1 sec-1, and a Km of 3.5 mM for GSH with a Kcat/Km of 1.51 x 10(3) M-1 sec-1. This is the second DHA reductase (after thioltransferase) isolated from human erythrocytes, but unlike thioltransferase, it has no thiol-disulfide oxido-reductase activity.
Kinetics, Erythrocytes, Humans, Electrophoresis, Polyacrylamide Gel, Protein Disulfide Reductase (Glutathione), Isoelectric Focusing, Chromatography, Ion Exchange, Oxidoreductases, Glutathione, Glutaredoxins
Kinetics, Erythrocytes, Humans, Electrophoresis, Polyacrylamide Gel, Protein Disulfide Reductase (Glutathione), Isoelectric Focusing, Chromatography, Ion Exchange, Oxidoreductases, Glutathione, Glutaredoxins
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