Trypsin activation of porcine procolipase. Kinetics of activation and effects on lipid binding

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Bibtex

@article{a81ab5a2d22f49a0b7dbce92b22d70ca,
title = "Trypsin activation of porcine procolipase. Kinetics of activation and effects on lipid binding",
abstract = "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.",
keywords = "Colipase, Kinetics, Lipid binding, Procolipase, Trypsin activation",
author = "Tadeusz Wieloch",
year = "1985",
month = "6",
day = "3",
doi = "10.1016/0014-5793(85)80741-9",
language = "English",
volume = "185",
pages = "63--66",
journal = "FEBS Letters",
issn = "1873-3468",
publisher = "Wiley-Blackwell",
number = "1",

}