Key result
The presence of apolipoprotein C-II increased the maximal activity of lipoprotein lipase on triolein particles, requiring 220 and 66 nM for half-maximal activity on small and large particles.
Population
Triolein particles stabilized by a phosphatidylcholine monolayer (small and large particles)
Design
Preclinical
Authors
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Offers mechanistic insight into apoC-II–LPL kinetics; leaves open relevance to human lipoprotein disorders.
Apolipoprotein C-II significantly increases the maximal activity of lipoprotein lipase on triolein particles, with enzyme kinetics dependent on the surface density of apoC-II and phosphatidylcholine.
Tajima et al. (1984) studied this question. Apolipoprotein C-II was evaluated on Lipoprotein lipase activity (hydrolysis of triolein). The presence of apolipoprotein C-II increased the maximal activity of lipoprotein lipase on triolein particles, requiring 220 and 66 nM for half-maximal activity on small and large particles.
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