小鼠肝脏金属硫蛋白-II的完整氨基酸序列。

Complete amino acid sequence of mouse liver metallothionein-II.

作者信息

Huang I Y, Kimura M, Hata A, Tsunoo H, Yoshida A

出版信息

J Biochem. 1981 Jun;89(6):1839-45. doi: 10.1093/oxfordjournals.jbchem.a133385.

DOI:10.1093/oxfordjournals.jbchem.a133385

Abstract

The complete amino acid sequence of thionein-II, one of the two major mouse liver thionein components, was determined. The main fragmentation of thionein-II, which consists of 61 amino acid residues, was accomplished by digesting the S-[14C]-carboxymethylated protein and the cyanogen bromide-treated oxidized protein with trypsin. The peptides obtained by papain digestion of S-[14C]carboxymethylated thionein-II were used to align the major tryptic peptides. The sequence was determined by a combination of automated and manual Edman degradation techniques. Remarkable structural homology is observed in mouse thionein-I, mouse thionein-II, and thioneins from man and horse.

摘要

已确定了小鼠肝脏中两种主要硫蛋白成分之一的硫蛋白-II的完整氨基酸序列。硫蛋白-II由61个氨基酸残基组成，其主要片段化是通过用胰蛋白酶消化S-[14C]-羧甲基化蛋白和溴化氰处理的氧化蛋白来完成的。木瓜蛋白酶消化S-[14C]羧甲基化硫蛋白-II得到的肽段用于比对主要的胰蛋白酶肽段。该序列是通过自动和手动埃德曼降解技术相结合来确定的。在小鼠硫蛋白-I、小鼠硫蛋白-II以及人和马的硫蛋白中观察到了显著的结构同源性。