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  • 标题:Purification and characterization of two initiation factors required for maximal activity of a highly fractionated globin mRNA translation system
  • 本地全文:下载
  • 作者:B Safer ; S L Adams ; W M Kemper
  • 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:1976
  • 卷号:73
  • 期号:8
  • 页码:2584-2588
  • DOI:10.1073/pnas.73.8.2584
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Two additional initiation factors (IF-M4 and IF-M5) have been purified and characterized both physically and biologically. IF-M4 is active as a single polypeptide chain with a molecular weight of 48,000. In contrast, IF-M5 is active as a complex with a molecular weight of about 500,000 and consists of seven major and several minor polypeptide components. Analysis of IF-M5 in two polyacrylamide gel electrophoresis systems indicated that one of the major polypeptide chains of IF-M5 was the 35,000 dalton subunit of IF-MP. This analysis also revealed that IF-M2A, IF-M3, and elongation factor 2 were present as minor components. Both IF-M4 and IF-M5 are required to achieve maximal activity in an assay system dependent on exogenous globin mRNA, but neither factor has been observed to stimulate model reactions that utilize artificial templates [poly(U) or AUG].
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