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虾夷扇贝(Patinopecten yessoensis)平滑肌肌球蛋白中调节性轻链a(RLC-a)的磷酸化作用

Phosphorylation of regulatory light chain a (RLC-a) in smooth muscle myosin of scallop, Patinopecten yessoensis.

作者信息

Sohma H, Yazawa M, Morita F

出版信息

J Biochem. 1985 Aug;98(2):569-72. doi: 10.1093/oxfordjournals.jbchem.a135311.

Abstract

One of the two regulatory light chains, RLC-a, of scallop smooth muscle myosin was fully phosphorylated by myosin light chain kinase of chicken gizzard muscle. The residue phosphorylated was Ser. It may be the Ser at number 11 from the N-terminal. The sequence of 9 residues around the Ser-11, QRATSNVFA, is identical with that around the phosphorylatable Ser of LC20 of chicken gizzard myosin. RLC-a was also phosphorylated slowly by cAMP-dependent protein kinase. The phosphorylation of RLC-a may be involved in the regulatory system for the catch contraction of scallop muscle.

摘要

扇贝平滑肌肌球蛋白的两条调节轻链之一RLC-α被鸡砂囊肌的肌球蛋白轻链激酶完全磷酸化。被磷酸化的残基是丝氨酸。它可能是N端第11位的丝氨酸。丝氨酸-11周围9个残基的序列QRATSNVFA与鸡砂囊肌球蛋白LC20可磷酸化丝氨酸周围的序列相同。RLC-α也被cAMP依赖性蛋白激酶缓慢磷酸化。RLC-α的磷酸化可能参与扇贝肌肉的强直收缩调节系统。

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