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- W2029089938 abstract "1. The relationship between fibre length and the Ca2+-activated ATPase (ATP phosphohydrolase, EC 3.6.1.3) of insect fibrillar muscle has been studied. 2. Low levels of Ca2+ and small degrees of fibre extension have been found to increase the ATPase activity. Either factor influences the sensitivity of the material to the other factor. 3. In insect fibrillar muscle, where the A filaments are continuous with the Z line, it is possible to strain the A filaments directly in the absence of permanent actin-myosin interactions. 4. The higher ATPase activity as a result of fibre elongation is accompanied by an increase in Ca2+ binding. 5. Small maintained length changes do not affect the rate of ATP breakdown catalyzed by glycerinated fibres from frog sartorius or rabbit psoas muscle. 6. The relevance of the findings to the mechanism of oscillatory contraction of insect fibrillar muscle is discussed." @default.
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- W2029089938 date "1967-03-01" @default.
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- W2029089938 title "The effect of Ca2+ and fibre elongation on the activation of the contractile mechanism of insect fibrillar flight muscle" @default.
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- W2029089938 doi "https://doi.org/10.1016/0005-2728(67)90152-1" @default.
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