Bile salt-stimulated lipase in human milk. Evidence that bile salt induces lipid binding and activation via binding to different sites.
Human milk bile salt-stimulated lipase ensures efficient triacylglycerol utilization in breast-fed newborns. For activity against long-chain triacylglycerol, primary bile salts are a prerequisite. Bile salts also protect the enzyme from inactivation by intestinal proteases. We have studied the effect of different bile salts on activation, protease protection, lipid binding, and enzyme inactivation, caused by an arginine modifying agent. Based on the results we propose a model involving two bile salt binding sites; one activation-site specific for primary bile salt, and another, less specific, lipid binding promoting site at which also secondary bile salt binds. Binding to this latter site induces binding of enzyme to emulsified substrates but binding promoting site at which also secondary bile salt binds. Binding to this latter site induces binding of enzyme to emulsified substrates but without subsequent lipolysis.
Department of Medical Biochemistry and Biophysics, University of Umeå, Sweden.
L
L
Bläckberg
O
O
Hernell
D001647:Bile Acids and Salts / Q000378:metabolism / Q000494:pharmacology*; D001665:Binding Sites; D003902:Detergents / Q000494:pharmacology; D004789:Enzyme Activation; D005260:Female; D006801:Humans; D007700:Kinetics; D008024:Ligands; D008049:Lipase / Q000378:metabolism*; D008895:Milk, Human / Q000201:enzymology*; D002787:Sterol Esterase
D001647:Bile Acids and Salts; D003902:Detergents; D008024:Ligands; C054784:bile salt-stimulated lipase; D002787:Sterol Esterase; D008049:Lipase