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• W1992069884 abstract "The properties of a specific adenosine nucleotide translocase from rat and pigeon heart mitochondria are similar to those of the system from liver. In particular, the Km for external ADP is very low, i.e. about 7 μm. The maximum activity of the translocase system, which was measured by following the exchange of adenine nucleotides across the mitochondrial membrane, or the Km of the system for ADP or ATP were not affected by Ca2+ concentration in the range 0.001 to 10 μm. Consequently the concentration change in sarcoplasmic Ca2+ that modifies the activities of several key metabolic enzymes plus the myofibrillar ATPase is unlikely to affect the activity of the translocase. However, in confirmation of previous work, higher concentrations of Ca2+ (up to 400 μm) increased considerably the exchange of the adenine nucleotides. There is some recent evidence that heart muscle mitochondria possess high affinity binding sites for Ca2+ in the mitochondrial membrane, which bind up to 300 nmol Ca2+ per g of heart muscle. It is emphasized that, if the adenine nucleotide translocase and the high affinity binding sites for Ca2+ are adjacent (or identical), the effects of the higher concentrations of Ca2+ on the translocase could be of considerable importance in control of the rate of translocation in heart muscle." @default.
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• W1992069884 date "1976-11-01" @default.
• W1992069884 modified "2023-09-27" @default.
• W1992069884 title "Effects of calcium ions on adenine nucleotide translocase from cardiac muscle" @default.
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• W1992069884 doi "https://doi.org/10.1016/0022-2828(76)90069-9" @default.
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