Action of rat liver cathepsin L on glucagon

Acta Biol Med Ger. 1981;40(9):1139-43.


The proteolytic specificity of cathepsin L on glucagon was determined. Major cleavages are found between Thr7 and Ser8, Asp15 and Ser16, and between Met27 and Asn28. The bonds Ser11-Lys12, Val23-Gln24, and Gln24-Trp25 are hydrolyzed to a relatively low extent only. Whereas cathepsin B hydroxyzes glucagon at the C-terminus by a peptidyldipeptidase mechanism, cathepsin L cleaves the same substrate clearly as endopeptidase.

Publication types

  • Comparative Study

MeSH terms

  • Animals
  • Cathepsin B
  • Cathepsin L
  • Cathepsins / metabolism*
  • Cysteine Endopeptidases
  • Endopeptidases*
  • Glucagon / metabolism*
  • Liver / enzymology
  • Peptide Fragments / analysis
  • Rats
  • Substrate Specificity


  • Peptide Fragments
  • Glucagon
  • Cathepsins
  • Endopeptidases
  • Cysteine Endopeptidases
  • Cathepsin B
  • Cathepsin L
  • Ctsl protein, rat