鸡骨骼肌肌球蛋白L-2轻链的氨基酸序列。

The amino acid sequence of the L-2 light chain of chicken skeletal muscle myosin.

作者信息

Suzuyama Y, Umegane T, Maita T, Matsuda G

出版信息

Hoppe Seylers Z Physiol Chem. 1980;361(2):119-27. doi: 10.1515/bchm2.1980.361.1.119.

DOI:10.1515/bchm2.1980.361.1.119

Abstract

The L-2 light chain of chicken skeletal muscle myosin was isolated and carboxymethylated. The L-2 light chain was digested with trypsin. The tryptic peptides thus obtained were separated and purified. The amino acid compositions and sequences of the tryptic peptides were analyzed. The primary structure of the L-2 light chain of chicken skeletal muscle myosin was determined by comparing the amino acid sequences of these tryptic peptides with the amino acid sequence of the L-2 light chain from rabbit skeletal muscle myosin.

摘要

分离并羧甲基化鸡骨骼肌肌球蛋白的L-2轻链。用胰蛋白酶消化L-2轻链。对由此获得的胰蛋白酶肽进行分离和纯化。分析胰蛋白酶肽的氨基酸组成和序列。通过将这些胰蛋白酶肽的氨基酸序列与兔骨骼肌肌球蛋白L-2轻链的氨基酸序列进行比较，确定鸡骨骼肌肌球蛋白L-2轻链的一级结构。