Studies on prolactin: 46. Preferential cleavage of the Arg125 ‐Leu126 peptide bond of ovine hormone with immobilized trypsin

Research output: Contribution to journalArticle

Abstract

Insoluble trypsin has been shown to attack preferentially some peptide bonds of ovine prolactin, within the large disulfide loop. The peptide bond most susceptible to immobilized trypsin was identified as the Arg125‐Leu126 of the ovine prolactin structure.

Original languageEnglish
Pages (from-to)212-214
Number of pages3
JournalInternational journal of peptide and protein research
Volume19
Issue number2
DOIs
Publication statusPublished - Feb 1982

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Keywords

  • biosynthesis
  • limited proteolysis

ASJC Scopus subject areas

  • Biochemistry

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