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• W2134148001 abstract "Glycerol-treated muscle fiber bundles were prepared mainly by storage in 50 per cent glycerol at −10°C for about 3 months. Their ATPase [EC 3.6. 1.3] activity was measured in the presence of 50 mM KCI, 2 to 3.35 mM MgCl2 and 20 mM Tris-maleate buffer at pH 7.0 and 25°C during an isometric contraction induced by ATP. Pyruvate kinase [EC 2.7.1.40] was coupled with myofibrillar ATPase, and the activity was measured by determining the amount of pyruvate liberated. The process of liberation of pyruvate from fiber bundles was linear with time in all the measurements. The ATPase activity of fiber bundles of about 300 μ in diameter and 2.2 to 2.6 μ in sarcomere length was independent of the concentration of phosphoenol pyruvate between 0.5 and 3.0 mM and the concentration of pyruvate kinase between 5 and 32 μg per ml, in the presence of 0.6mM ATP. Furthermore, in the presence of 1.0 mM phosphoenol pyruvate and 65 μg pyruvate kinase per ml, the activity was scarcely affected by an increase in concentration of ATP from 0.6 to 5.0 mM. The ATPase activity of fiber bundles of 250 to 310 μ in diameter and 4.2 to 5.3 μ in sarcomere length was independent of the concentration of ATP between 0.22 and 0.77 mM or of that of phosphoenol pyruvate between 0.5 and 1.0 mM, if the amounts of other constituents were sufficient. The activity of fiber bundles of 240 to 310 μ in diameter and 0.8 to 0.9 μ in sarcomere length was not affected by increase in the concentration of pyruvate kinase from 25 to 250 μg per ml or that of ATP from 2.35 to 5.0 mM. The activity in 0.6 mM ATP was almost equal to that in 2.35 mM ATP. Thus, it was concluded that the diffusion of ATP and phosphoenol pyruvate was not the limiting factor in the hydrolysis of ATP, if fiber bundles of less than 300 μ in diameter were used in the presence of at least 0.6 mM ATP and 1.0 mM phosphoenol pyruvate. The fiber bundles showed the maximum activity of 100 μmoles pyruvate per minute per g of protein at sarcomere lengths of 2.0 to2.5 μ. As the sarcomere length increased beyond 2.5 μ, the activity decreased and reached about 30 uμmoles pyruvate per minute per g of protein at sarcomere lengths of more than 4 μ. In the region where the sarcomere length was less than 2.0 μ, the ATPase activity decreased as the sarcomere length decreased, and, at a sarcomere length of 1 μ, it showed a quarter to a third of the maximum activity. These results suggested that both ATPase activity and tension development are coupled with the movement of myosin filaments past actin filaments. The maximum activity observed at sarcomere lengths of 2.0 to 2.5 μ was only one fourth of the activity of the actomyosin type of isolated acto-myosin. The dependence on Ca++ concentration of the ATPase of glycerol-treated muscle fiber bundles, which had been stored for about 3 months, was investigated at fixed sarcomere lengths of 2.0 to 2.6 μ. When Ca++ was removed by EGTA, the activity was about 48 μmoles pyruvate per minute per g of protein, and in the presence of 1 mM Ca++ it was 116 μmoles pyruvate per minute per g of protein. The concentration of Ca++ for the half maximum activation was about 0.04 μM. In the presence of 1 to 2mM EGTA, the activity of fiber bundles stored for 3 to 13 days was only 17 μmoles pyruvate per minute per g of protein, and that of those stored for about 9 months was 126 μmoles pyruvate per minute per g of protein." @default.
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• W2134148001 date "1968-01-01" @default.
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• W2134148001 title "Dependence of Activity of Myofibrillar ATPase on Sarcomere Length and Calcium Ion Concentration***" @default.
• W2134148001 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a128736" @default.
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