Nov 1, 1975

On the interactions between pancreatic lipase and colipase and the substrate, and the importance of bile salts

Journal of Lipid Research
B Borgström

Abstract

The interactions between pancreatic lipase and colipase and the substrate and the effect of bile salts on these interactions have been investigated by the use of kinetic experiments and studies on the semiquantitative phase distribution of lipase and colipase activities. The results suggest that lipase binds to hydrophobic interfaces with partial irreversible inactivation. Bile salts in the range of micellar concentrations and above a pH of about 6.5 displace lipase from this binding, resulting in a reversible in activation. At pH values below about 6.5, lipase binds strongly to the substrate even in the presence of bile salt, and a low activity peak is seen around pH 5.5. This is the result of the binding of lipase to the "supersubstrate" and the activity of the catalytic site. In the presence of bile salt, colipase promotes the binding of lipase to the "supersubstrate" but not to other hydrophobic interfaces, and catalytic activity is reestablished. Kinetic data indicate that the binding between colipase and lipase in the presence of substrate is strong and occurs in an approximately stoichiometric relationship.

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Mentioned in this Paper

Bile Acid Measurement
Taurine, Monopotassium Salt
Pancreatic lipase
Colipases
Plasma Protein Binding Capacity
Triacylglycerol Lipase Measurement
Enzyme Activity
Binding (Molecular Function)
Deoxycholic Acid, Sodium Salt, 12beta-Isomer
PNLIP gene

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