Specificity of lipoprotein lipase and hepatic lipase toward monoacylglycerols varying in the acyl composition.
We report here that both the hepatic lipase and lipoprotein lipase demonstrate specificity towards the acyl group present on monoacylglycerols. We found that unsaturated glycerides are more readily degraded than saturated glycerides. However, the basis for this specificity appears to be different for each enzyme. The activity of the hepatic lipase, but not the lipoprotein lipase, could be stimulated by Triton X-100 and phosphoglycerides. We interpret these results to show that while both the lipoprotein lipase and hepatic lipase are sensitive to the physical state of the substrate (as shown by fluorescence depolarization), the lipoprotein lipase also has a low affinity for monoacylglycerols that contain a saturated acyl group. In the course of this study we also obtained evidence that some type of phase separation occurs when mixtures of saturated and unsaturated monoacylglycerols are prepared.
D000818:Animals; D002250:Carbon Radioisotopes; D002417:Cattle; D003902:Detergents; D005260:Female; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D008071:Lipoprotein Lipase / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D008892:Milk / Q000201:enzymology; D017830:Octoxynol; D011092:Polyethylene Glycols; D051381:Rats; D013379:Substrate Specificity; D014316:Tritium
D002250:Carbon Radioisotopes; D003902:Detergents; D014316:Tritium; D011092:Polyethylene Glycols; D017830:Octoxynol; D008049:Lipase; D008071:Lipoprotein Lipase