Substrate conformation directs selective enzymic cleavage of β-lipotropin into β-endorphin

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

It is shown that whilst the Arg51-Trp52 and Arg60-Tyr61 peptide bonds of β-lipotropin are preferentially split by trypsin-Sepharose in aqueous solution, in a secondary structure promoting environment the Arg60-Tyr61 peptide bond is almost exclusively cleaved. It is suggested that the specificity of intracellular precursor processing may be directed by the conformation of the substrate.

Original languageEnglish
Pages (from-to)1089-1093
Number of pages5
JournalBiochemical and biophysical research communications
Volume93
Issue number4
DOIs
Publication statusPublished - Apr 29 1980

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Substrate conformation directs selective enzymic cleavage of β-lipotropin into β-endorphin'. Together they form a unique fingerprint.

  • Cite this