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

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Trypsin activation of porcine procolipase. Kinetics of activation and effects on lipid binding. / Wieloch, Tadeusz.

I: FEBS Letters, Vol. 185, Nr. 1, 03.06.1985, s. 63-66.

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T1 - Trypsin activation of porcine procolipase. Kinetics of activation and effects on lipid binding

AU - Wieloch, Tadeusz

PY - 1985/6/3

Y1 - 1985/6/3

N2 - 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.

AB - 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.

KW - Colipase

KW - Kinetics

KW - Lipid binding

KW - Procolipase

KW - Trypsin activation

U2 - 10.1016/0014-5793(85)80741-9

DO - 10.1016/0014-5793(85)80741-9

M3 - Article

VL - 185

SP - 63

EP - 66

JO - FEBS Letters

JF - FEBS Letters

SN - 1873-3468

IS - 1

ER -