Hydrolysis of rat chylomicron acylglycerols: a kinetic model.
A quantitative model describing the kinetics of hydrolysis of rat chylomicron acylglycerols by bovine milk lipoprotein lipase has been developed using data from studies on rat lymph chylomicrons containing doubly labeled acylglycerols. The detailed analysis indicates that, in addition to hydrolysis from tri- to di-, di- to mono-, and monoacylglycerol to glycerol, and apparently direct hydrolysis pathway of tri- to monoacylglycerol is also present. This accounts for the transient accumulation of monoacylglycerol seen in some of the experiments. For most hydrolysis steps, a Michaelis-Menten mechanism adequately describes the rate of hydrolysis as a function of lipoprotein lipase concentration. A higher order, more complex mechanism, however, is necessary for the apparent tri- to monoacylglycerol hydrolysis pathway. A mathematical function that describes the way free fatty acid released can control the rates of hydrolysis, and how the presence of the binding sites for free fatty acid on albumin in the incubation medium can modulate this, in included. The model simultaneously satisfies the kinetics of hydrolysis for tri-,  di-, and monoacylglycerol together with the kinetics of the glycerol and fatty acid moieties for a wide range of albumin and lipoprotein lipase concentrations.
D000818:Animals; D002417:Cattle; D002914:Chylomicrons; D004075:Diglycerides; D005260:Female; D005989:Glycerides; D006868:Hydrolysis; D007700:Kinetics; D008071:Lipoprotein Lipase / Q000378:metabolism*; D008892:Milk / Q000201:enzymology; D008954:Models, Biological; D051381:Rats; D014280:Triglycerides
D002914:Chylomicrons; D004075:Diglycerides; D005989:Glycerides; D014280:Triglycerides; D008071:Lipoprotein Lipase