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- W1997593668 abstract "1. Microsomes from heart muscle yield two components by flotation in polyanion-containing sucrose gradients. Both components have ATPase activity, but only that in the heavier component is stimulated by calcium ions. Under the same conditions, microsomes from skeletal muscle yield only a single component and this has ATPase activity which is stimulated by Ca2+. 2. The light component of heart muscle microsomes has a low content of esterase and NADH-cytochrome c reductase and a high level of non-specific nucleoside phosphate phosphohydrolase activities. In these respects, it resembles previously described plasma membrane preparations from liver and cultured fibroblasts. Non-specific nucleoside triphosphate phosphohydrolase activity is not affected by calcium ions or the sulphydryl reagent, mersalyl, but is inhibited by azide. 3. The heavy component of heart muscle microsomes contains almost all of the esterase and NADH-cytochrome c reductase. A Ca2+-dependent ATPase is coincident with these activities. This ATPase resembles the sarcotubular ATPase of skeletal muscle with regard to optimum concentration of Ca2+, sensitivity to mersalyl and insensitivity to azide, but differs in its specificity for ATP and a lower apparent affinity for ATP." @default.
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- W1997593668 date "1971-03-01" @default.
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- W1997593668 title "Resolution of fragments of plasma and sarcotubular membranes in heart muscle microsomes" @default.
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- W1997593668 doi "https://doi.org/10.1016/0005-2736(71)90355-5" @default.
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