Maita T, Konno K, Maruta S, Norisue H, Matsuda G
Department of Biochemistry, Nagasaki University School of Medicine.
J Biochem. 1987 Nov;102(5):1141-9. doi: 10.1093/oxfordjournals.jbchem.a122152.
The amino acid sequence of the essential light chain (abbreviated as SHLC) of adductor muscle myosin from Ezo giant scallop (Patinopecten yessoensis) was determined by conventional methods. The light chain was composed of 156 amino acid residues with proline and lysine as its amino and carboxyl termini, respectively. Comparing this sequence with that of the SHLC from bay scallop (Aquipecten irradians), only 5 amino acid substitutions were recognized. The sequence homology between scallop and squid SHLCs was 53.7%. On the other hand, a partially fragmented SHLC "modified SHLC" reported by Konno and Watanabe (J. Biochem. 98, 141-148 (1985) was prepared by chymotryptic digestion of the scallop myosin in the presence of EDTA, and was assigned as the carboxyl-terminal 106-residue peptide of the SHLC. This may suggest that the regulatory light chain covers the amino-terminal region of the SHLC in the myosin molecule.
采用常规方法测定了北紫扇贝（Patinopecten yessoensis）闭壳肌肌球蛋白必需轻链（简称为SHLC）的氨基酸序列。该轻链由156个氨基酸残基组成，其氨基末端和羧基末端分别为脯氨酸和赖氨酸。将该序列与海湾扇贝（Aquipecten irradians）的SHLC序列进行比较，仅发现5个氨基酸替换。扇贝和鱿鱼SHLC之间的序列同源性为53.7%。另一方面，Konno和Watanabe（《生物化学杂志》98, 141 - 148 (1985)）报道的部分片段化的SHLC“修饰SHLC”是在EDTA存在的情况下，通过胰凝乳蛋白酶消化扇贝肌球蛋白制备的，并被确定为SHLC的羧基末端106个残基的肽段。这可能表明调节轻链覆盖了肌球蛋白分子中SHLC的氨基末端区域。
