[Properties of phospholipase A2 from inner and outer mitochondrial membranes]

The catalytic properties of membrane-bound phospholipase A2 from inner and outer mitochondrial membranes were studied. Differences were found in the properties of phospholipase A2 during the hydrolysis of both endogenous and exogenous substrates, i.e. the dependence of the hydrolysis rate on pH, temperature, bivalent metal ion concentrations and EDTA. It was demonstrated that purification and adsorption immobilization of the inner mitochondrial membrane enzyme on biospecific adsorbent cause changes in the enzyme catalytic properties. The role of phospholipase A2 microenvironment in the manifestation of the enzyme activity and catalytic properties is discussed.