载脂蛋白C-II的N-α-棕榈酰（56-79）片段对脂蛋白脂肪酶的激活作用。

Activation of lipoprotein lipase by N-alpha-palmitoyl (56-79) fragment of apolipoprotein C-II.

作者信息

Balasubramaniam A, Rechtin A, McLean L R, Jackson R L, Demel R A

出版信息

Biochem Biophys Res Commun. 1986 Jun 30;137(3):1041-8. doi: 10.1016/0006-291x(86)90330-x.

Abstract

The effect of apolipoprotein C-II (apoC-II) and a synthetic fragment of apoC-II corresponding to residues 56-79 on the lipoprotein lipase (LpL) catalyzed hydrolysis of trioleoylglycerol in a monolayer of egg phosphatidylcholine and of dipalmitoylphosphatidylcholine vesicles was examined. Synthetic peptide 56-79, which does not associate with lipid, did not activate LpL at surface pressures greater than 30 mN/m; apoC-II is active up to 34 mN/m. However, acylation of the NH2-terminus of peptide 56-79 with palmitoyl chloride gave nearly identical LpL activating properties as compared to apoC-II. We conclude that at high surface pressures the lipid-binding region of apoC-II (residues 44-55) plays an essential role in LpL activation.

摘要

研究了载脂蛋白C-II（apoC-II）以及与apoC-II 56 - 79位残基相对应的合成片段对脂蛋白脂肪酶（LpL）催化的三油酰甘油在单层卵磷脂和二棕榈酰磷脂酰胆碱囊泡中的水解作用。不与脂质结合的合成肽56 - 79在表面压力大于30 mN/m时不激活LpL；apoC-II在高达34 mN/m时具有活性。然而，用棕榈酰氯对肽56 - 79的NH2末端进行酰化后，其LpL激活特性与apoC-II几乎相同。我们得出结论，在高表面压力下，apoC-II的脂质结合区域（44 - 55位残基）在LpL激活中起关键作用。