Trypsin activation of porcine procolipase

FEBS Letters

Wieloch, Tadeusz¹ 

[1] Department of Physiological Chemistry, University of Lund, S-220 07 Lund, Sweden

关键词: Colipase;    Procolipase;    Trypsin activation;    Kinetics;    Lipid binding;   

DOI  :  10.1016/0014-5793(85)80741-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The kinetics of trypsin activation of pancreatic procolipase was investigated and the pH dependence of the binding of procolipase and colipase to a tributyrine-bile salt interface studied. The K _m was 0.06 mM and K _cat 8 s⁻¹, and was of the same order of magnitude as for the activation of pancreatic zymogens. At basic pH values colipase had a higher affinity for the tributyrine-bile salt interface as compared to procolipase. The trypsin activation of procolipase ensures a rapid degradation of dietary lipids in the intestine.

【 授权许可】

Unknown