[Fractionation of inner and outer mitochondrial membranes in rat liver (author's transl)].

Mitochondrial membranes of rat liver were fractionated into inner and outer membranes by osmotic shock. Purity of the inner and outer membrane subfractions was examined by estimating marker enzyme activities of succinate-cytochrome c reductase and monoamine oxidase, respectively. Monoamine oxidase activity in the outer membrane subfraction was found to be 21.90 mmumoles of benzaldehyde produced/min./mg. protein and 1.57 mmumoles in the inner membranes, whereas succinate-cytochrome c reductase activity was 13.4 and 33.0 mmumoles/min./mg. protein, respectively. These results indicate higher purity of each membrane fraction obtained.