Autolysis of proproteinase E in bovine procarboxypeptidase A ternary complex gives rise to subunit III

Roger Pascual, Josep Vendrell, Francesc X. Avilés, Jacques Bonicel, Catherine Wicker, Antoine Puigserver

Research output: Contribution to journalArticleResearchpeer-review

19 Citations (Scopus)

Abstract

Extracts of bovine pancreatic tissue are shown by HPLC to contain two distinct ternary complexes of procarboxypeptidase A (subunit I), chymotrypsinogen C (subunit II) and either proproteinase E or subunit III. It is shown that proproteinase E in the complex generates subunit III by removal of 13 N-terminal residues when the former is allowed to autolyze in solution or when catalytic amounts of isolated active proteinase E are added to it. Autolysis of proproteinase E was accompanied by the loss of potential activity towards specific synthetic substrates and occurred at a higher rate in pancreatic juice than in pancreatic tissue extracts, even when both were processed in the presence of serine protease inhibitors. We conclude that subunit III (also called truncated protease E) is an autolytic product of proproteinase E and not an ab initio component of the native ternary complex. © 1990.
Original languageEnglish
Pages (from-to)37-41
JournalFEBS Letters
Volume277
DOIs
Publication statusPublished - 17 Dec 1990

Keywords

  • Autolysis
  • Bovine pancreas
  • Subunit III
  • Zymogen E

Fingerprint Dive into the research topics of 'Autolysis of proproteinase E in bovine procarboxypeptidase A ternary complex gives rise to subunit III'. Together they form a unique fingerprint.

Cite this