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National Institute of Environmental Health Sciences

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Publication Detail

Title: Purification and characterization of a glutathione dependent dehydroascorbate reductase from human erythrocytes.

Authors: Xu, D P; Washburn, M P; Sun, G P; Wells, W W

Published In Biochem Biophys Res Commun, (1996 Apr 5)

Abstract: 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.

PubMed ID: 8660320 Exiting the NIEHS site

MeSH Terms: Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel; Erythrocytes/enzymology*; Glutathione/metabolism*; Humans; Isoelectric Focusing; Kinetics; Oxidoreductases/blood*; Oxidoreductases/isolation & purification*; Protein Disulfide Reductase (Glutathione)*; Research Support, U.S. Gov't, P.H.S.

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