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

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.

authors

Xu DP,Washburn MP,Sun GP,Wells WW

doi

10.1006/bbrc.1996.0555

subject

Has Abstract

pub_date

1996-04-05 00:00:00

pages

117-21

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(96)90555-0

journal_volume

221

pub_type

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