Trypsin activation of porcine procolipase. Kinetics of activation and effects on lipid binding.
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 Km was 0.06 mM and kcat 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.
D000818:Animals; D003089:Colipases / Q000378:metabolism*; D004792:Enzyme Precursors; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008823:Micelles; D011498:Protein Precursors / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D013552:Swine; D013657:Taurodeoxycholic Acid / Q000378:metabolism; D014280:Triglycerides / Q000378:metabolism*; D014357:Trypsin / Q000494:pharmacology*
D003089:Colipases; D004792:Enzyme Precursors; D008823:Micelles; D011498:Protein Precursors; D011506:Proteins; D014280:Triglycerides; D013657:Taurodeoxycholic Acid; C037107:procolipase; D014357:Trypsin; C005830:tributyrin