Parés X, Farrés J, Vallee B L
Biochem Biophys Res Commun. 1984 Mar 30;119(3):1047-55. doi: 10.1016/0006-291x(84)90880-5.
Human placenta contains a single detectable isozyme of alcohol dehydrogenase that has been isolated and characterized. It migrates toward the anode on starch gel electrophoresis and can be stained with pentanol but not ethanol as substrate. Its kinetic and molecular characteristics are identical with those of the recently discovered chi-ADH (Class III) isozyme from human liver. Placental ADH is present in the cytosol of this organ in small amounts, 6 mg/kg fresh tissue. It oxidizes ethanol very slowly--even at ethanol concentrations that would reflect intoxication when found in serum. Thus, placental alcohol dehydrogenase cannot play a significant role in the ethanol metabolism of pregnant women.
人胎盘含有一种可检测到的酒精脱氢酶同工酶，该同工酶已被分离并鉴定。在淀粉凝胶电泳中它向阳极迁移，并且可以用戊醇作为底物进行染色，但不能用乙醇作为底物染色。其动力学和分子特征与最近从人肝脏中发现的Ⅲ类同工酶（chi-ADH）相同。胎盘酒精脱氢酶在该器官的胞质溶胶中含量很少，为6毫克/千克新鲜组织。它氧化乙醇的速度非常缓慢——即使在血清中发现时乙醇浓度会反映中毒的情况下也是如此。因此，胎盘酒精脱氢酶在孕妇的乙醇代谢中不能发挥重要作用。
