The primary structure of human β-lipotropin. Further peptide sequencing resolves the controversy and suggests the existence of only one human β-lipotropin

N. G. Seidah, K. L. Hsi, M. Chrétien, E. Barat, A. Patthy, L. Graf

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Human β-lipotropin isolated in Hungary from frozen pituitary glands was purified by high-performance liquid chromatography in Canada. The amino acid sequence of the first 30 residues was determined. Trypsin, trypsin/papain, and trypsin/thermolysin fragments were obtained for the disputed region containing residues 9-25 of β-lipotropin. Their amino acid composition and sequence established beyond doubt that only one human β-lipotropin sequence is present. These results suggest the presence of only one gene coding for human pro-opiomelanocortin, the precursor of adrenocorticotropin and β-endorphin and resolve the controversy over the sequence of human β-lipotropin.

Original languageEnglish
Pages (from-to)267-272
Number of pages6
JournalFEBS letters
Volume147
Issue number2
DOIs
Publication statusPublished - Oct 18 1982

Keywords

  • HPLC purification
  • Human β-lipotropin
  • Sequence

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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