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- W1987758410 abstract "1. Isotonic swelling and shrinking of the mitochondria of Saccharomyces cerevisiae in the presence of valinomycin and subsequent sucrose gradient centrifugation resulted in the separation of the inner and outer mitochondrial membranes. Succinate: cytochrome c reductase and malate dehydrogenase served as markers for the inner membrane and the matrix, respectively, adenylate kinase for the intermembrane space. 2. The outer membrane fraction is characterized by the activities of both antimycin A-insensitive NADH: cytochrome c reductase and kynurenine hydroxylase. The latter is shown to be exclusively bound to the outer mitochondrial membrane in yeast. Kynurenine hydroxylase exhibits a sharp pH optimum at about pH 7.4. Yeast mitochondria fail to show monoamine oxidase activity. 3. The products of mitochondrial and cytoplasmic protein synthesis in Saccharomyces cerevisiae were each selectively labelled in vivo. The fractions obtained after membrane separation were characterized by their 3H to 14C ratio. The outer membrane of yeast mitochondria is not pulse-labelled by radioactive leucine incorporation in the presence of cycloheximide and hence is apparently not synthesized by the mitochondial protein synthesizing system. More than one third of the inner membrane protein is synthesized on mitrochondrial ribosomes. 4. As estimated from enrichment in enzyme activity and in specific radioactivity, the outer membrane fraction contains 6–8%, the inner about 30% of the total protein in yeast mitochondria. 5. Intact mitochondria, outer and inner membranes exhibit densities of 1.173 g/cm3, 1.084 g/cm3 and 1.190 g/cm3, respectively 6. All mitochondrial subfractions obtained after membrane separation were examined for their morphological appearance by electron microscopy." @default.
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- W1987758410 date "1972-09-01" @default.
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- W1987758410 title "Membrane separation and biogenesis of the outer membrane of yeast mitochondria" @default.
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- W1987758410 doi "https://doi.org/10.1016/0005-2736(72)90315-x" @default.
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