Watanabe B
School of Allied Medical Sciences, Nagasaki University.
Biol Chem Hoppe Seyler. 1989 Jun;370(6):549-58. doi: 10.1515/bchm3.1989.370.1.549.
The amino-acid sequence of a short subfragment-2 in the amino-terminal portion of subfragment-2 (S-2) derived from adult chicken skeletal muscle myosin was completely determined. Peptides cleaved by cyanogen bromide and by lysyl endopeptidase of S-carboxymethylated S-2, and hydrolytic peptides obtained with trypsin or dilute acetic acid of larger CNBr fragments were isolated and sequenced. This region was composed of 257 amino-acid residues, and hydrophobic and charged residue repeat units were found highly conserved and with a periodicity in 7 or 28 residues. This sequence of the short S-2 fragment of chicken skeletal muscle myosin was compared with the sequence of chicken and rat embryonic skeletal muscle myosins, rabbit skeletal and rabbit cardiac muscle myosin (alpha-myosin heavy chain), and 95.3%, 86.8%, 89.9% and 94.2% sequence identities were observed, respectively.
已完全确定了源自成年鸡骨骼肌肌球蛋白的亚片段-2（S-2）氨基末端部分的短亚片段-2的氨基酸序列。分离并测序了经溴化氰裂解以及经S-羧甲基化S-2的赖氨酰内肽酶裂解得到的肽段，以及用胰蛋白酶或稀乙酸处理较大溴化氰片段得到的水解肽段。该区域由257个氨基酸残基组成，发现疏水和带电荷残基重复单元高度保守且具有7或28个残基的周期性。将鸡骨骼肌肌球蛋白短S-2片段的这一序列与鸡和大鼠胚胎骨骼肌肌球蛋白、兔骨骼肌和兔心肌肌球蛋白（α-肌球蛋白重链）的序列进行了比较，分别观察到序列同一性为95.3%、86.8%、89.9%和94.2%。
