Shinomiya M, Jackson R L
Biochim Biophys Acta. 1984 Jul 6;794(2):177-82. doi: 10.1016/0005-2760(84)90144-9.
The effect of phospholipid organization on the lipoprotein lipase-catalyzed hydrolysis of dimyristoylphosphatidylcholine was examined with sonicated vesicles and Triton X-100 or lysomyristoylphosphatidylcholine solubilized lipid. Triton X-100-dimyristoylphosphatidylcholine substrates were prepared at various ratios of detergent to phospholipid so as to produce lipid structures varying from bilayers to micelles. Apolipoprotein C-II, the activator protein for lipoprotein lipase, enhanced the rate of the lipoprotein lipase-catalyzed hydrolysis of dimyristoylphosphatidylcholine for each substrate tested. Although the absolute rate of lipoprotein lipase catalysis was different for each, the factor (the ratio of lipoprotein lipase activity with apolipoprotein C-II to that without the activator protein) was nearly constant, with a value of approximately 16. We conclude that the enhancement of lipoprotein lipase activity by apolipoprotein C-II is independent of the physical form of the phospholipid substrate.
利用超声处理的囊泡以及用 Triton X - 100 或溶血肉豆蔻酰磷脂酰胆碱增溶的脂质，研究了磷脂组织对脂蛋白脂肪酶催化的二肉豆蔻酰磷脂酰胆碱水解的影响。以去污剂与磷脂的不同比例制备 Triton X - 100 - 二肉豆蔻酰磷脂酰胆碱底物，以产生从双层到胶束的不同脂质结构。载脂蛋白 C - II 是脂蛋白脂肪酶的激活蛋白，它提高了所测试的每种底物的脂蛋白脂肪酶催化的二肉豆蔻酰磷脂酰胆碱水解速率。尽管每种底物的脂蛋白脂肪酶催化的绝对速率不同，但该因子（有载脂蛋白 C - II 时的脂蛋白脂肪酶活性与无激活蛋白时的脂蛋白脂肪酶活性之比）几乎恒定，值约为 16。我们得出结论，载脂蛋白 C - II 对脂蛋白脂肪酶活性的增强与磷脂底物的物理形式无关。
