作者: Fumi MORITA , Shuhei KONDO
DOI: 10.1093/OXFORDJOURNALS.JBCHEM.A134054
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摘要: Myosin purified from the smooth muscle of scallop adductor contains two kinds regulatory light chain, chain a (RLC-a) and b (RLC-b) (Kondo, S. & Morita, F. (1981) J. Biochem. 90, 673). The myosin was fractionated by salting out with ammonium sulfate, samples containing chains different molar ratios were obtained. ATPase activities fractions determined. From analysis dependence activity on ratio chains, we concluded that three species having combinations chains: one has RLC-a (aa), another RLC-b (bb), third each (ab). order these estimated as (aa) less than (bb) Distribution in inside, translucent portion to outside, opaque examined means one- two-dimensional gel electrophoreses. content about 1 mol per SH-light independent muscle. markedly dependent muscle--about 0.2 innermost 0.7 portion. sum both contents 1.5 where catch contraction is notable. are discussed.