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Updated: Aug 12, 2026

Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases
Published on: October 10, 2020
Glutathione reductase from human erythrocytes. Catalytic properties and aggregation
Abstract:
The catalytic properties of glutathione reductase from human erythrocytes have been studied over a range of buffer conditions and substrate concentrations. This study provides optimal conditions for determining the basic kinetic parameters of the enzyme. The catalytic behaviour of glutathione reductase is consistent with spatially separated binding sites for its substrates. In certain assays anomalies were observed which are correlated with an inactivation of the enzyme by NADPH. Concurrent sedimentation experiments showed that NADPH promoted aggregation of the enzyme. Both inactivation and aggregation could be connected with oxidation of thiols at the active site. The relation of the properties of glutathione reductase to cellular conditions is discussed.
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