Elzinga M, Collins J H
Proc Natl Acad Sci U S A. 1977 Oct;74(10):4281-4. doi: 10.1073/pnas.74.10.4281.
A peptide having 92 amino acid residues and a calculated molecular weight of 10,478 was isolated from a cyanogen bromide digest of rabbit skeletal muscle myosin. It contained both proline and Ntau-methylhistidine, indicating that it arose from the portion of the heavy chain that folds to form most of the globular head of the myosin molecule. The amino acid sequence of the peptide included the two sulfhydryl groups whose alkylation modifies myosin's catalytic properties: SH-2 at position 11 in the peptide, and SH-1 at position 21. This proximity in the sequence means that SH-1 and SH-2 must be relatively close together in myosin, and several lines of evidence suggest that this region is near the catalytic or actin binding site(s) of myosin.
从兔骨骼肌肌球蛋白的溴化氰消化产物中分离出一种含有92个氨基酸残基、计算分子量为10478的肽。它同时含有脯氨酸和N-甲基组氨酸，这表明它源自重链中折叠形成肌球蛋白分子大部分球状头部的部分。该肽的氨基酸序列包括两个巯基，其烷基化会改变肌球蛋白的催化特性：肽中第11位的SH-2和第21位的SH-1。序列上的这种邻近性意味着SH-1和SH-2在肌球蛋白中必定相对靠近，并且多条证据表明该区域靠近肌球蛋白的催化或肌动蛋白结合位点。
