In human postheparin plasma, lipoprotein lipase activity elutes primarily with lipoproteins slightly larger than low-density lipoproteins, suggesting an association with apo B- and apo E-containing particles.
Observational (n=11)
No
LPL activity in postheparin plasma appears to be bound to remnants of chylomicrons and very low density lipoproteins, providing insight into lipoprotein metabolism.
Studies were designed to explore the association of lipoprotein lipase (LPL) and hepatic triglyceride lipase (HTGL) activities with lipoproteins in human postheparin plasma (PHP). The major peak of LPL activity after gel filtration of PHP eluted after the triglyceride-rich lipoproteins and just before the peak of low density lipoprotein (LDL) cholesterol. When PHP contained chylomicrons, an additional peak of LPL activity eluted in the void volume of the column. Most HTGL activity eluted after the LDL and preceded the elution of high density lipoprotein cholesterol. LPL activity in preheparin plasma eluted in the same position, relative to lipoproteins, as did LPL in PHP. Gel filtration of purified human milk LPL mixed with plasma or isolated LDL produced a peak of activity eluting before LDL. During gel filtration of PHP in high salt buffer (1 M NaCl) or after isolation of lipoproteins by ultracentrifugation in high salt density solutions, most of the lipase activity was not associated with lipoproteins. LPL activity was removed from PHP by elution through immunoaffinity columns containing antibodies to apolipoprotein (apo) B and apo E. Since lipoproteins in PHP have undergone prior in vivo lipolysis, LPL activity in PHP may be bound to remnants of chylomicrons and very low density lipoproteins.
Goldberg et al. (1986) conducted an observational in Healthy volunteers and hyperlipoproteinemia (n=11). Intravenous heparin vs. Preheparin plasma was evaluated on Elution position of lipoprotein lipase (LPL) and hepatic triglyceride lipase (HTGL) activities relative to lipoproteins. In human postheparin plasma, lipoprotein lipase activity elutes primarily with lipoproteins slightly larger than low-density lipoproteins, suggesting an association with apo B- and apo E-containing particles.