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

FEBS Letters

Pascual, Roger²  Puigserver, Antoine¹  Wicker, Catherine¹  Vendrell, Josep²  Avilés, Francesc X.²  Bonicel, Jacques¹ 

[1] Centre de Biochimie et Biologie Moléculaire, CNRS, 31 Ch.J. Aiguier, 13402 Marseile Cedex 9, France;Departament de Bioquimica (Fac. Ciències) & Institut de Biologin Fondamental, Universitat Autónoma de Barcelona, 08193 Bellaterra (Barcelona, Spain

关键词: Zymogen E;    Bovine pancreas;    Autolysis;    Subunit III;    PPE;    proproteinase E;    PE-α;    active proteinase E generated by tryptic activation;    PE-β;    inactive proteinase E generated by N-terminal truncation of the zymogen by active proteinase E;    HPLC;    high-performance liquid chromatography;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/0014-5793(90)80804-R

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown