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pubmed-article:4086487pubmed:abstractTextThe concept that creatine phosphokinase is bound to the outer surface of the heart mitochondrial inner membrane originated from observations that the enzyme is retained by water-swollen heart mitochondria and by digitonin-treated heart mitochondria suspended in isotonic sucrose. The present study establishes that digitonin-treated mitochondria release creatine phosphokinase in isotonic KCl, and other investigators have reported an identical response for the water-swollen organelles. These observations suggest that mitochondrial creatine phosphokinase is not bound to the outer surface of the inner membrane at a site adjacent to the adenine nucleotide translocase under physiologic conditions.lld:pubmed
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pubmed-article:4086487pubmed:articleTitleEffects of ionic strength and sulfhydryl reagents on the binding of creatine phosphokinase to heart mitochondrial inner membranes.lld:pubmed
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pubmed-article:4086487pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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