Pieroni G, Verger R
Eur J Biochem. 1983 May 16;132(3):639-44. doi: 10.1111/j.1432-1033.1983.tb07411.x.
We studied the effect of glycerides on pancreatic phospholipase A2 hydrolysis of mixed monomolecular films of trioctanoylglycerol/1,2-didodecanoyl-sn-glycero-3-phosphocholine with the technique of Piéroni and Verger [(1979) J. Biol. Chem. 254, 10090-10094]. The quantity of enzyme adsorbed to the interface was concomitantly determined with [3H]amidinated phospholipase. At phospholipid packing above the critical penetration pressure, triacylglycerol stimulates phosphatidylcholine hydrolysis to a great extent. On the other hand, the activity of pancreatic phospholipase A2 on a mixed film is inhibited by the action of pancreatic lipase. Interface binding of phospholipase A2 to the lipid substrate does not imply activity.
我们采用皮耶罗尼和韦尔热的技术（[1979年，《生物化学杂志》254卷，10090 - 10094页]）研究了甘油酯对三辛酰甘油/1,2 - 二癸酰 - sn - 甘油 - 3 - 磷酸胆碱混合单分子膜的胰腺磷脂酶A2水解作用。用[3H]酰胺化磷脂酶同时测定吸附到界面的酶量。在磷脂堆积高于临界渗透压力时，三酰甘油在很大程度上刺激磷脂酰胆碱水解。另一方面，胰腺脂肪酶的作用会抑制胰腺磷脂酶A2在混合膜上的活性。磷脂酶A2与脂质底物的界面结合并不意味着有活性。
