嗜热脂肪芽孢杆菌两种小核糖体蛋白的氨基酸序列。

The amino acid sequence of two small ribosomal proteins from Bacillus stearothermophilus.

作者信息

Tanaka I, Kimura M, Kimura J, Dijk J

出版信息

FEBS Lett. 1984 Jan 30;166(2):343-6. doi: 10.1016/0014-5793(84)80109-x.

PMID:6420194

Abstract

The low-Mr proteins (tentatively called protein I and II) were purified from 2 M NaCl extracts of the Bacillus stearothermophilus ribosome. Their amino acid sequences have been determined from the peptides obtained by digestion with trypsin, chymotrypsin, and pepsin, and by cleavage with CNBr, using the micro-DABITC/PITC double-coupling method [FEBS Lett. (1978) 93, 205-214]. Protein I contains 56 residues and has an Mr of 6514. Protein II had 37 residues with an Mr of 4361. The amino acid sequence of protein I shows significant similarity to L32 from E. coli, whereas that of protein II is slightly, if at all, related to ribosomal protein L34 from E. coli.

摘要

低分子量蛋白质（暂称为蛋白质I和II）是从嗜热脂肪芽孢杆菌核糖体的2M NaCl提取物中纯化得到的。它们的氨基酸序列已通过用胰蛋白酶、胰凝乳蛋白酶和胃蛋白酶消化以及用溴化氰裂解所获得的肽段来确定，采用的是微量DABITC/PITC双偶联法[《欧洲生物化学学会联合会快报》（1978年）93卷，205 - 214页]。蛋白质I含有56个残基，分子量为6514。蛋白质II有37个残基，分子量为4361。蛋白质I的氨基酸序列与大肠杆菌的L32有显著相似性，而蛋白质II的氨基酸序列与大肠杆菌的核糖体蛋白L34即便有联系也很微弱。