摘要
采用人肝微粒体温育实验 ,根据 CYP45 0 1A2特异性抑制法及 HPL C机电化学分析仪检测结果 ,发现 :1催化 MT在肝脏羟化和去甲基反应的 CYP45 0异构酶确证是 CYP45 0 1A2。 2 CYP45 0 1A2催化 MT6位羟化反应的Km 是 (4.48± 1.49) μm ol/ L (x± s) ,Vmax是 (13.83± 2 .5 2 ) pm ol/ (m g protein· min) (x±s)。 3催化 MT5位上 O-去甲基主要是 CYP45 0 1A2 ,还有 2 C19参与 ,其 Km值分别为 0 .0 30 μmol/ L 和 8.796 μmol/ L,Vmax分别是 0 .338pm ol/(mg protein· min)和 3.16 7pm ol/ (mg protein·m in)
On the basis of in vitro experiment of human liver microsome incubation with melatonin (MT), two main degrade metabolites of melatonin (MT), 6 hydroxymelatonin (6 HMT) and N acetylserotonin (N A5HT) were analyzed by using high performance liquid chromatography (HPLC) combined with electrochemical detection (ED). It was found: (1) The CYP450 isoenzyme catalyzing MT biotransformation in liver was approved to be CYP450 1A2. (2) The Km of CYP P50 1A2 responsible for the catalyzation of 6 hydroxylation of MT was 4.48±1.49 μmol/L, Vmax was 13.83±2.52 pmol/(mg protein.min). (3) Both CYP450 1A2 and 2C19, mainly CYP450 1A2, catalyzed the 5 O desmethyl of MT with the Km being 0.030 μmol/L and 8.796 μmol/L, and Vmax being 0.338 pmol/(mg.min) and 3.167 pmol/(mg.min), respectively.
出处
《同济医科大学学报》
CSCD
2000年第2期102-104,107,共4页
Acta Universitatis Medicinae Tongji
