Radulovic L L, LaFerla J J, Kulkarni A P
Biochem Pharmacol. 1986 Oct 15;35(20):3473-80. doi: 10.1016/0006-2952(86)90614-3.
The ability of human placental glutathione S-transferase (GSHTr) to metabolize methyl parathion (MeP) was examined. MeP was found to be a substrate for both partially purified pre-term and highly purified term placental GSHTr. The characterization of the reaction by high performance liquid chromatography revealed the presence of desmethyl parathion (DesMeP) as the sole metabolite. Term placental GSHTr activity towards MeP ranged from 2.22 to 3.53 nmoles DesMeP formed X min-1 X mg-1 while an activity of 0.60 to 1.12 nmoles DesMeP formed X min-1 X mg-1 was observed with the pre-term placental enzyme. The absence of the O-dearylation reaction by pre-term and term placental GSHTr represents a major species- and/or tissue-specific difference.
对人胎盘谷胱甘肽S-转移酶(GSHTr)代谢甲基对硫磷(MeP)的能力进行了检测。发现MeP是部分纯化的早产胎盘和高度纯化的足月胎盘GSHTr的底物。通过高效液相色谱对反应进行表征,结果显示仅存在去甲基对硫磷(DesMeP)作为代谢产物。足月胎盘GSHTr对MeP的活性范围为每分钟每毫克形成2.22至3.53纳摩尔DesMeP,而早产胎盘酶的活性为每分钟每毫克形成0.60至1.12纳摩尔DesMeP。早产和足月胎盘GSHTr不存在O-脱烷基化反应,这代表了主要的物种和/或组织特异性差异。