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Journal of Lipid Research, Vol 26, 824-830, Copyright © 1985 by Lipid Research, Inc.

ARTICLES

Kinetic properties of human milk bile salt-activated lipase: studies using long chain triacylglycerol as substrate

CS Wang and DM Lee

Studies on the hydrodynamic properties of human milk bile salt- activated lipase (BAL) indicated that it is a monomer with molecular weight of 107,000. The presence of taurocholate (1 mM) did not lead to an association of the enzyme. The enzyme had a basal activity with trioctanoylglycerol and with shorter chain, but not with longer chain, monoacid triacylglycerols. Based on kinetic analyses, we suggest that the BAL-catalyzed lipolysis of long-chain triacylglycerol can be described to follow a compulsory sequential mechanism. The initial interaction of BAL with the activator (taurocholate) leads to a conformational change of the enzyme which facilitates the further interaction with the long chain triacylglycerol substrate in forming the enzyme-bile salt-substrate ternary complex. We also suggest that the binding of BAL with substrate involves direct interaction of the active site with the fatty acyl-chain of the triacylglycerol rather than with nonspecific hydrophobic interactions at the emulsion interface.
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				C. J. O'Connor, P. A.G. Butler, and B. M. Sutton Bile-Salt-Stimulated Human Milk Lipase: Interaction with Proteins Journal of Bioactive and Compatible Polymers, January 1, 1988; 3(4): 390 - 402. [Abstract] [PDF]