作者: A Y Lu , D M Jerina , W Levin
DOI: 10.1016/S0021-9258(17)40311-5
关键词:
摘要: 1. The substrate specificity of membrane-bound and purified epoxide hydrase from rat liver microsomes has been studied. Both enzyme preparations catalyzed the hydration a variety alkene oxidase as well arene oxides several polycyclic aromatic hydrocarbons. 2. Unlike enzyme, rate for most substrates by was constant only 1 or 2 min. addition dilauroyl phosphatidylcholine heated to incubation mixture extended linearity reaction. 3. When were used source apparent Km values many dependent on amount used. benzo(a)pyrene 11,12-oxide substrate, independent concentration but added lipid concentration. Thus, in absence presence this at below its critical micelle concentration, observed remained constant. However, when greater than value increased linearly with These results are consistent model based partition lipid-soluble between aqueous medium.