IDENTITY OF PURIFIED MONOACYLGLYCEROL LIPASE, PALMITOYL-COA HYDROLASE AND ASPIRIN-METABOLIZING CARBOXYLESTERASE FROM RAT-LIVER MICROSOMAL FRACTIONS - A COMPARATIVE-STUDY WITH ENZYMES PURIFIED IN DIFFERENT LABORATORIES
IDENTITY OF PURIFIED MONOACYLGLYCEROL LIPASE, PALMITOYL-COA HYDROLASE AND ASPIRIN-METABOLIZING CARBOXYLESTERASE FROM RAT-LIVER MICROSOMAL FRACTIONS - A COMPARATIVE-STUDY WITH ENZYMES PURIFIED IN DIFFERENT LABORATORIES
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DOI：
10.1042/bj2320479
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发表时间：
1985-01-01
影响因子：
4.1
通讯作者：
HEYMANN, E
中科院分区：
文献类型：
--
作者：
MENTLEIN, R;BERGE, RK;HEYMANN, E
从挪威和德国实验室的大鼠肝微粒体中分离纯化的两种羧酸酯酶进行了比较。在许多早期文献中，挪威的酶制剂被归类为棕榈酰辅酶A水解酶(EC3.1.2.2)，而德国的制剂被命名为单酰基甘油脂肪酶(EC 3.1.1.23)或酯酶PI 6.2/6.4(非特异性羧酸酯酶，EC 3.1.1)。两种纯化酶制剂的抗血清具有交叉反应。这两种蛋白质在十二烷基硫酸钠/聚丙烯酰胺凝胶电泳法中共同迁移。用棕榈酰辅酶A和丁酸苯酯两种底物测定，两种酶对镁、钙和双-(4-硝基苯基)磷酸表现出相同的抑制特性。结果表明，这两种酯酶制剂是相同的。免疫沉淀和抑制实验证实，该酶不同于大鼠肝脏胞浆和线粒体的棕榈酰辅酶A水解酶。
Two purified carboxylesterases that were isolated from a rat liver microsomal fraction in a Norwegian and a German laboratory were compared. The Norwegian enzyme preparation was classified as palmitoyl-CoA hydrolase (EC3.1.2.2) in many earlier papers, whereas the German preparation was termed monoacylglycerol lipase (EC 3.1.1.23) or esterase pI 6.2/6.4 (non-specific carboxylesterase, EC 3.1.1.). Antisera against the two purified enzyme preparations were cross-reactive. The two proteins co-migrate in sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Both enzymes exhibit identical inhibition characteristics with Mg2+, Ca2+ and bis-(4-nitrophenyl) phosphate if assayed with the two substrates palmitoyl-CoA and phenyl butyrate. It is concluded that the two esterase preparations are identical. However, immunoprecipitation and inhibition experiments confirm that this microsomal lipase differs from the palmitoyl-CoA hydrolases of rat liver cytosol and mitochondria.