Abstract
The 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 digitonintreated 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.
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Wenger, W.C., Murphy, M.P., Brierley, G.P. et al. Effects of ionic strength and sulfhydryl reagents on the binding of creatine phosphokinase to heart mitochondrial inner membranes. J Bioenerg Biomembr 17, 295–303 (1985). https://doi.org/10.1007/BF00751106
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DOI: https://doi.org/10.1007/BF00751106