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- W2015783725 abstract "Abstract Native tropomyosin and fragmented sarcoplasmic reticulum from crayfish tail muscle have been obtained in a pure state. After isoelectric precipitation, the former system yields two biologically active components, troponin and tropomyosin. Troponin binds calcium and can dissociate into three subunits of molecular weight 54 000, 29 000 and 16 000. The tropomyosin monomer has a molecular weight of 40 000. Desensitized actomyosin becomes calcium sensitive in the presence of native tropomyosin or tropomyosin plus troponin. The properties of crayfish fragmented sarcoplasmic reticulum (ATPase activity, calcium binding and uptake, inhibition of actomyosin superprecipitation) are characteristic of a calcium pump. Comparison with the regulatory system of rabbit skeletal muscle reveals many similarities between crayfish and mammalians; indeed crayfish fragmented sarcoplasmic reticulum or native tropomyosin can influence the calcium sensitivity of rabbit actomyosin." @default.
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- W2015783725 date "1974-11-01" @default.
- W2015783725 modified "2023-09-26" @default.
- W2015783725 title "Regulatory proteins of crayfish tail muscle" @default.
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- W2015783725 doi "https://doi.org/10.1016/0005-2728(74)90153-4" @default.
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