Nishijima J, Okamoto M, Nakaguchi K, Ogawa M, Yamano T, Mori T
Gen Pharmacol. 1985;16(3):177-82. doi: 10.1016/0306-3623(85)90065-5.
Human erythrocyte ghost membranes were incubated with human pancreatic phospholipase A2 [EC 3.1.1.4] in the presence of gabexate mesilate (FOY, ethyl 4-(6-guanidinohexanoyloxy)-benzoate methanesulfonate) in Tris-buffered saline (10 mM Tris-HCl, 150 mM NaCl, 2 mM CaCl2, pH 7.4). Membrane phospholipids were extracted by chloroform-isopropanol, 7:11 (v/v), and separated by thin-layer chromatography. Gabexate mesilate at a concentration of 400 microM caused a 50% inhibition of the enzyme-mediated hydrolysis of membrane phospholipids. When phosphatidylcholine micelles were incubated with the enzyme in the presence of gabexate mesilate, the mode of inhibition of the enzyme action by the drug appeared to be noncompetitive and Ki of gabexate mesilate for phospholipase A2 was 0.77 mM.
将人红细胞血影膜与人类胰腺磷脂酶A2 [EC 3.1.1.4] 在甲磺酸加贝酯（FOY，4-(6-胍基己酰氧基)苯甲酸乙酯甲磺酸盐）存在的情况下，于Tris缓冲盐溶液（10 mM Tris-HCl、150 mM NaCl、2 mM CaCl2，pH 7.4）中孵育。用氯仿-异丙醇（7:11，v/v）提取膜磷脂，并通过薄层色谱法进行分离。浓度为400 microM的甲磺酸加贝酯导致酶介导的膜磷脂水解受到50%的抑制。当磷脂酰胆碱微团在甲磺酸加贝酯存在的情况下与该酶孵育时，药物对酶作用的抑制模式似乎是非竞争性的，甲磺酸加贝酯对磷脂酶A2的Ki为0.77 mM。
