Hydrolysis of plasma triacylglycerol-rich lipoproteins from immature and laying hens (Gallus domesticus) by lipoprotein lipase in vitro.

Very-low-density (VLD) lipoproteins and portomicrons were isolated from the plasma of immature and laying hens and their size, lipid composition and susceptibility to hydrolysis by lipoprotein lipase were compared. In agreement with other studies, VLD lipoproteins from laying hens were found to be smaller and have a different lipid composition than VLD lipoproteins from immature hens. Portomicrons from immature and laying hens had mean diameters of about 150 nm and similar lipid compositions. Hydrolysis of VLD lipoproteins from immature hens, and portomicrons from immature and laying hens, proceeded rapidly until at least 40% of the substrate had been used. In contrast only 1--15% of laying-hen VLD-lipoprotein triacylglycerol was readily hydrolysis occurred slowly. The limited susceptibility of laying-hen VLD lipoproteins appeared to be due to their low content of lipoprotein lipase activator apoprotein, which occurred despite an abundance of activator in the high-density lipoproteins of laying-hen plasma. The results provide further evidence that the liver of the laying hen synthesizes specialized lipoproteins. Their limited susceptibility to hydrolysis by lipoprotein lipase is probably a major factor in ensuring transport of lipid to yolk rather than to other tissues. The form of transport of dietary lipid, however, is similar in immature and laying hens.