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- W1561569456 abstract "Summary Protein turnover was studied in cerebral mitochondria purified by centrifugation on a continuous sucrose density-gradient, and in the component membranes, prepared by two different procedures. As judged by electron microscopy the purified mitochondrial preparations were free of lysosomal contamination and were readily split by phospholipase treatment to yield good preparations of inner membrane. Three aspects of protein turnover in the intact mitochondria and their component membranes were studied: (1) distribution of enzymes involved in protein breakdown, (2) incorporation of labeled amino acids, and (3) protein and amino acid composition. Mitochondria and their membrane components exhibited intrinsic proteolytic activity, sufficient to account for the known rates of cerebral protein turnover; outer membranes contained a slightly higher concentration of aminopeptidase (Leu-Gly-Gly) and acid proteinase (Hb). The chief site of amino acid incorporation resided in the membrane components, which accounted for the major portion of the total radioactivity; incorporation into inner membrane exceeded that into the outer membrane by 35% in vivo and 56% in vitro. Differences between the membrane components based on their disc-gel patterns and content of amino acids, in addition to the data on rates of protein breakdown and incorporation, indicate different biogenetic origins for the proteins present in the submitochondrial components." @default.
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- W1561569456 date "1970-03-01" @default.
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- W1561569456 title "Protein metabolism in cerebral mitochondria" @default.
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- W1561569456 doi "https://doi.org/10.1016/0006-8993(70)90331-8" @default.
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