Glutathione reductase from human erythrocytes: catalytic properties and aggregation
DJ Worthington, MA Rosemeyer - European Journal of …, 1976 - Wiley Online Library
DJ Worthington, MA Rosemeyer
European Journal of Biochemistry, 1976•Wiley Online LibraryThe catalytic properties of glutathione reductase from human erythrocytes have been
studied over a range of buffer conditions and substrate concentrations. This study provides
cptimal conditions for determinime 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 …
studied over a range of buffer conditions and substrate concentrations. This study provides
cptimal conditions for determinime 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 …
The catalytic properties of glutathione reductase from human erythrocytes have been studied over a range of buffer conditions and substrate concentrations. This study provides cptimal conditions for determinime 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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