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- W2024495236 abstract "Abstract 1. 1. Sarcolemmal tubules were prepared from frog skeletal muscle by hypotonie disruption of muscle cell segments with water (pH 7.6), washing with dilute solutions of ATP and isolation by density-gradient centrifugation. 2. 2. Sarcolemmal preparations had an ATPase activity stimulated by Mg 2+ or Ca 2+ ions. Both enzyme activities were inhibited by Na + and K + and by combinations of these monovalent cations. Mg 2+ -stimulated ATPase activity, with or without Na + and K + , was not affected by ouabain. 3. 3. The optimal levels of Mg 2+ or Ca 2+ at I = 0.05, pH 7.4 and 3 mM ATP were 3 and 12 mM, respectively. With equimolar ATP and Mg 2+ or Ca 2+ , the respective K m values were 2.75 × 10 −3 M and 3.57 × −3 M. 4. 4. Mg 2+ -stimulated ATPase activity was completely inhibited by o.1 % deoxycholate but only slightly by 1 mM EGTA and 2,4-dinitrophenol. 5. 5. Sarcolemmal preparations did not accumulate 45 Ca in the presence of ATP, Mg 2+ and oxalate. 6. 6. The Sarcolemmal ATPase, while showing some resemblance to ‘basal’ ATPase in its response to Mg 2+ and Ca 2+ , is demonstrably a different enzyme system. 7. 7. Sarcolemmal preparations were free of mitochondria as indicated by the absence of cytochrome oxidase activity. 8. 8. Actomyosin contamination of Sarcolemmal preparations was assessed by extraction with 0.6 M KCl, testing for super-precipitation on addition of ATP and measuring Ca 2+ and EDTA-activated ATPase activities at I = 0.6, pH 7.4. Extraction and enzymatic results showed that the Sarcolemmal preparations contained about 20% actomyosin or similar protein. 9. 9. After extraction with 0.6 M KCl, sarcolemmal preparations retained most of their ATPase activity." @default.
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- W2024495236 date "1975-03-01" @default.
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- W2024495236 title "Adenosinetriphosphatase activity of isolated sarcolemmal tubules of frog skeletal muscle" @default.
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