[Solubilization of mitochondria-bound rat skeletal muscle hexokinase isoenzyme II by glucose-6-phosphate]

Solubilization of bound to outer mitochondrial membrane hexokinase isoenzyme II by glucose-6-phosphate (G-6-P) has been studied. Dissociation of the enzyme-membrane complex was analyzed in both active (in the presence of reaction substrates) and inactive states. The magnitude of the complex dissociation constants was determined under G-6-P action in the presence and absence Mg.ATP. Besides, some kinetic parameters of hexokinase isoenzyme II in its free and bound forms were estimated. It is suggested that the mechanism of dissociation of the hexokinase-membrane complex by G-6-P is coupled with the kinetic mechanism of the reaction catalyzed by hexokinase isoenzyme II.