Open AccessGlutathione Reductase from Human Erythrocytes
Author(s) -
WORTHINGTON David J.,
ROSEMEYER Michael A.
Publication year - 1976
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1976.tb10654.x
Subject(s) - glutathione , glutathione reductase , chemistry , enzyme , catalysis , substrate (aquarium) , biochemistry , reductase , biophysics , biology , glutathione peroxidase , ecology
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.