Characterization of human chylomicrons.

Apolipoprotein and lipid composition of differently sized chylomicrons from healthy volunteers was determined. During their intravasal catabolism the chylomicrons lose triacylglycerol and apolipoproteins. Decreasing particle size results in a loss of apolipoprotein C and apolipoprotein E peptides and an increase in apolipoproteins B and A-I, which constitutes more than 20% of the moiety of small chylomicrons. The C peptides do not seem to behave as a functional entity. Apolipoprotein C-III, the inhibitor of lipolytic activities, is catabolized independently of the other C peptides. Albumin constitutes about 15-25% of the protein moiety of all chylomicrons. The different chylomicron fractions were incubated with lipolytic activities of lipoprotein lipase and hepatic triacylglycerol lipase. At lower substrate concentrations the reactions were of first-order. Large chylomicrons were the favored substrate for both enzymes with Michaelis Menten constant Km = 1.1 mM for hepatic triacylglycerol lipase and 0.48 mM for lipoprotein lipase. After incubation with hepatic triacylglycerol lipase or lipoprotein lipase the shape of chylomicrons differs from that of control particles as demonstrated by electron microscopy. C peptides were completely dissociated and found in the infranatant. In the enzyme assay with triolein gum arabic substrate several apolipoproteins showed an influence on the activities of hepatic triacylglycerol lipase and lipoprotein lipase. Apolipoprotein C-III peptides were the most effective inhibitors of both enzymes. Also, apolipoprotein A-II, A-I and apolipoprotein C-I inhibited lipoprotein lipase activity, whereas only apolipoprotein A-II was able to decrease hepatic triacylglycerol activity.