Sep 14, 1976

Human erythrocyte glutathione reductase. I. Purification and properties

Biochimica Et Biophysica Acta
K NakashimaK Yamauchi

Abstract

1. Glutathione reductase (NAD(P)H:oxidized-glutathione oxidoreductase, EC. 1.6.4.2) from human erythrocytes was purified 49 000-fold with an overall yield of 15% and a 280/460 nm absorbance ratio of 6.03. The procedure used was the method of Worthington and Rosemeyer modified by addition of heating and recrystallization. 2. It was concluded from the results of purification, electrofocusing and inhibition studies that glutathione reductase is a single enzyme which used both NADPH and NADH as hydrogen donors. 3. Apoenzyme cross-reacts with the antibody to the holoenzyme but has a slightly reduced affinity to the antibody. Apoenzyme can be removed from the hemolysate by heating and centrifugation without loss of holoenzyme. 4. Indirect immunological assay of the specific activity of the erythrocyte glutathione reductase is possible in the enzyme saturated with FAD.

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Mentioned in this Paper

Apoenzymes
NADH
Glutathione Measurement
Centrifugation
GSR gene
Purification Aspects
Specimen Type - Erythrocytes
Metabolic Inhibition
Isoelectric Focusing
GSR

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