Sodek J, Hodges R S, Smillie L B
J Biol Chem. 1978 Feb 25;253(4):1129-36.
Amino acid sequence analysis of the large cyanogen bromide fragment (residues 142 to 281) derived from the COOH-terminal half of the mixed tropomyosin population of rabbit skeletal muscle has been carried out. The isolation and sequence analysis of peptides derived from chymotryptic digests and from tryptic digests of the maleylated fragment permitted the alignment of the complete sequence except for the assignment of acids or amides at residues 142, 144, and 145. Selected peptides from a Myxobacter 495 alpha-lytic protease digest have confirmed certain overlaps. Based on previously published data the sequence can be extended to residue 284, the COOH-terminal end of the protein. In fourteen positions, amino acid substitutions have been observed. In one of these (residue 199) the sequence evidence indicates a minimum of four different polypeptide chains in the mixed tropomyosin population. The assignment of particular amino acid residues to these positions for the major alpha-component of rabbit skeletal tropomyosin has been based on the relative recoveries of peptides containing different residues in these positions.
对源自兔骨骼肌混合原肌球蛋白群体羧基末端一半的大溴化氰片段（第142至281位氨基酸残基）进行了氨基酸序列分析。对马来酰化片段的胰凝乳蛋白酶消化产物和胰蛋白酶消化产物衍生的肽段进行分离和序列分析，除了确定第142、144和145位氨基酸残基是酸还是酰胺外，其余部分的完整序列得以排列。粘细菌495α-裂解蛋白酶消化产物中的选定肽段证实了某些重叠。根据先前发表的数据，该序列可延伸至第284位氨基酸残基，即该蛋白质的羧基末端。已观察到14个位置存在氨基酸替换。其中一个位置（第199位氨基酸残基）的序列证据表明，混合原肌球蛋白群体中至少存在四条不同的多肽链。兔骨骼肌原肌球蛋白主要α-组分在这些位置的特定氨基酸残基的确定，是基于这些位置含有不同残基的肽段的相对回收率。
