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- W2024471004 abstract "Abstract The outer membrane was isolated from sonicated heavy beef heart mitochondria according to the procedure of Green et al. (1). By repeated hypotonic and detergent washing, citric cycle enzyme activity (α-ketoglutarate dehydrogenase) could be removed completely from the outer membrane preparation. By this procedure the rotenone-insensitive DPNH cytochrome c reductase (RIDCR) and the monoamine oxidase activities could not be washed away from the membrane fragments; instead, both activities were concentrated greatly when compared to their starting specific activities. Concomitantly, during the purification procedure inner membrane contamination, as measured by cytochromes a + a3 content, could be removed by differential centrifugation. Phospholipid constituted approximately 45% of the total dry weight, and the cholesterol level was also found to be greatly enhanced. Electron microscopically, negatively stained preparations of the partially purified mitochondrial outer membrane appeared to consist exclusively of smooth-surfaced, rounded membrane fragments, having a thickened edge. When examined by polyacrylamide gel electrophoresis, the partially purified outer membrane preparation exhibited several small protein components with one major protein component dominating the electrophoretic trace." @default.
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- W2024471004 date "1971-03-01" @default.
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- W2024471004 title "Partial purification of the outer membrane fraction from sonicated heavy beef heart mitochondria" @default.
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- W2024471004 doi "https://doi.org/10.1016/0003-9861(71)90181-0" @default.
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