Huang I Y, Yoshida A
J Biol Chem. 1977 Nov 25;252(22):8217-21.
The amino acid sequence of thionein-I, a major mouse liver thionein, is presented. Thionein-I is a single chain polypeptide which consists of 61 amino acid residues and has the amino acid composition Cys20, Asp3, Asn1, Thr5, Ser9, Gln1, Pro2, Gly5, Ala5, Val2, Met1, Lys7, with N-acetylmethionine and alanine as NH2- and COOH-terminal amino acids, respectively. Automated sequence analysis of a major cyanogen bromide peptide consisting of 60 amino acid residues, as well as characterization of the peptides obtained from trypsin and papain digestion, led to the elucidation of the complete primary structure of this protein. Remarkable structural homology is observed between the mouse thionein-I and the equine renal thionein-1B (Kojima, Y., Berger, C., Vallee, B.L., and Kägi, J.H.R. (1976) Proc. Natl. Acad. Sci. U.S.A. 73, 3413-3417).
本文给出了小鼠肝脏主要硫蛋白硫蛋白-I的氨基酸序列。硫蛋白-I是一种单链多肽，由61个氨基酸残基组成，其氨基酸组成为：20个半胱氨酸、3个天冬氨酸、1个天冬酰胺、5个苏氨酸、9个丝氨酸、1个谷氨酰胺、2个脯氨酸、5个甘氨酸、5个丙氨酸、2个缬氨酸、1个甲硫氨酸、7个赖氨酸，其氨基端氨基酸为N-乙酰甲硫氨酸，羧基端氨基酸为丙氨酸。对一个由60个氨基酸残基组成的主要溴化氰肽段进行自动序列分析，以及对胰蛋白酶和木瓜蛋白酶消化所得肽段的表征，从而阐明了该蛋白质的完整一级结构。在小鼠硫蛋白-I和马肾硫蛋白-1B之间观察到显著的结构同源性（小岛洋、伯杰、瓦利、B.L.和凯吉、J.H.R.（1976年）《美国国家科学院院刊》73，3413 - 3417）。
