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• W2089099060 abstract "Two types of myosin isolated from ordinary (fast) and dark (slow) muscles of carp were examined by ATPase and in vitro motility assays. Vmax of the ATPase activity and sliding velocity of ordinary myosin showed 1.6 and 1.5 times higher activities than those of dark myosin, whereas those of mammalian fast myosin were much higher, 3 to 10 times, than those of slow myosin. Although ordinary myosin had almost identical activities to those of mammalian fast myosin, activities of dark myosin was twice of those of mammalian slow myosin. This high motile activity of dark myosin can account for the physiological role of dark muscle in cruising of fish. By comparing Km of the actin-activated ATPase activity, ordinary myosin was appeared to have higher affinity to F-actin than dark myosin, and this was confirmed by the binding assay of HMM or S-1 of carp myosin to F-actin. Investigation of myosin assembly by electron microscopy and the centrifugation assay revealed that ordinary myosin assembled much poorly than dark myosin or mammalian fast myosin. This phenomenon may reflect characteristic cellular function of fish skeletal muscle." @default.
• W2089099060 created "2016-06-24" @default.
• W2089099060 creator A5073905687 @default.
• W2089099060 date "2005-09-01" @default.
• W2089099060 modified "2023-10-16" @default.
• W2089099060 title "Biochemical Properties of Ordinary and Dark Muscle Myosin from Carp Skeletal Muscle" @default.
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• W2089099060 doi "https://doi.org/10.1093/jb/mvi121" @default.
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