Kinetic properties of human VLDL substrate for membrane-supported lipoprotein lipase and inhibitory effect of lipid peroxide to the lipase activity was studied. Activity of lipoprotein lipase supported on vascular surface was measured by perfusion of isolated rat heart. Human VLDL was used as substrate. Lipid peroxide was prepared by ultraviolet irradiation and air oxidation of Methyl Linolenate at 40℃. Lipid[ peroxide value was quantified by a simple fluorometric assay (Yagi's method). Maximal reaction velocity (Vmax) of healthy human VLDL was 0.037 μmol/min After incubation of VLDL with the albumin solution containing 3.9nmol/ml of lipid peroxide,…