Urea‐gradient gel electrophoresis studies on the association of procarboxypeptidases A and B, proproteinase E, and their tryptic activation products

FEBS Letters

Vilanova, M.¹  Burgos, F.J.¹  Cuchillo, C.M.¹  Avilés, F.X.¹ 

[1] Departament de Bioquimíca, Facultat de Cièmies i Institut de Biologia Fonamental ‘Vicent Villar Palasí’, Universitat Autònoma de Barcelona, Bellaterra, Barcelona, Spain

关键词: Procarboxypeptidase;    Proproteinase E;    Activation product;    Association study;    Pig pancreas;    PCPA;    PCPB;    CPA;    CPB;    procarboxypeptidases and carboxypeptidases A and B;    PPE and PE;    proproteinase E and proteinase E;    asA and asB;    severed activation segments of procarboxypeptidase A and B;    respectively;   

DOI  :  10.1016/0014-5793(85)80023-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Monomeric procarboxypeptidase A (PCPA) and isolated proproteinase E (PPE), both from pig pancreas, were shown by means of electrophoresis on transverse urea gradients (0–9 M) to form a very stable complex, identical to their natural binary complex. Although the complex is maintained by the interaction of both active regions, the activation segment of PCPA participates directly in the binding. Procarboxypeptidase B (PCPB) also associates with PPE, but in this case the complex shows low stability. In contrast with carb-oxypeptidases A that strongly bind to their corresponding severed activation segments, no interaction was observed between carboxypeptidase B and its severed activation segment. The above results give some insight into several characteristics of the structure and activation properties of pancreatic PCPA and PCPB.

【 授权许可】

Unknown