首页    期刊浏览 2024年11月24日 星期日
登录注册

文章基本信息

  • 标题:Human Parathyroid Hormone: Amino-Acid Sequence of the Amino-Terminal Residues 1-34
  • 本地全文:下载
  • 作者:H. B. Brewer ; T. Fairwell ; R. Ronan
  • 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:1972
  • 卷号:69
  • 期号:12
  • 页码:3585-3588
  • DOI:10.1073/pnas.69.12.3585
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Human parathyroid hormone has been isolated in highly purified form from human parathyroid adenomas. The primary sequence of the amino-terminal 34 residues of the human hormone was obtained by automated degradation with a Beckman Sequencer. The phenylthiohydantoin amino acids were identified by gas chromatography and mass spectrometry. The first 34 residues of human parathyroid hormone differ from the bovine hormone by six residues, and from the porcine hormone by five residues. The amino-terminal residue is serine, similar to the porcine parathyroid hormone; bovine parathyroid hormone contains an amino-terminal alanine. Human parathyroid hormone contains two methionine residues, similar to the bovine species, whereas porcine parathyroid hormone contains a single methionine residue. Amino-acid residues in the first 34 that are unique to the human sequence include an asparagine at position 16, glutamine at position 22, lysine at position 28, and a leucine at position 30.
  • 关键词:automated Edman degradation ; mass spectrometry ; calcium metabolism ; metabolic bone disease
国家哲学社会科学文献中心版权所有