首页    期刊浏览 2024年11月07日 星期四
登录注册

文章基本信息

  • 标题:Primary structure of elongation factor Tu from Escherichia coli
  • 本地全文:下载
  • 作者:K Arai ; B F Clark ; L Duffy
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1980
  • 卷号:77
  • 期号:3
  • 页码:1326-1330
  • DOI:10.1073/pnas.77.3.1326
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:The amino acid sequence of elongation factor Tu (EF-Tu) from Escherichia coli has been determined. EF-Tu is a single-chain polypeptide composed of 393 amino acids (Mr 43,225 for the species bearing COOH-terminal serine). The NH2-terminal serine is acetylated, and lysine-56 is partially methylated. The sites of facile tryptic cleavage are at arginines 44 and 58 and at lysine-263. The cysteinyl residues associated with aminoacyl-tRNA and guanosine nucleotide binding activities are residues 81 and 137, respectively. The COOH-terminal amino acid is heterogenous in that analyses of the COOH-terminal peptides isolated from different EF-Tu preparations gave position 393 as glycine and serine in ratios (Gly/Ser) ranging from about 0.7 to 3.
国家哲学社会科学文献中心版权所有