Duncan R J, Kline J E, Sokoloff L
Biochem J. 1976 Mar 1;153(3):561-6. doi: 10.1042/bj1530561.
A method for obtaining electrophoretically homogeneous rat liver alcohol dehydrogenase (EC 1.1.1.1) at a specific activity of 2-2.5 mumol/min per mg of protein is presented. Anti-sera prepared against the purified enzyme inhibit alcohol dehydrogenase by up to 75% and cause precipitation of virtually all the enzyme. The antisera were shown by immunoelectrophoresis of a partially purified liver homogenate to be specifically directed against alcohol dehydrogenase and were used to demonstrate that the alcohol dehydrogenases of rat brain and liver share common antigens. The total activity of alcohol dehydrogenase in rat brain homogenates is normally quite low, with as much as 10% of the total activity attributable to the activity in the blood contained within the brain; in cases of severe liver damage (induced experimentally with carbon tetrachloride) this contribution may rise to as much as 60%.
本文介绍了一种获得电泳纯大鼠肝脏乙醇脱氢酶(EC 1.1.1.1)的方法,其比活性为每毫克蛋白质2 - 2.5微摩尔/分钟。针对纯化酶制备的抗血清可抑制乙醇脱氢酶达75%,并使几乎所有的酶沉淀。通过对部分纯化的肝脏匀浆进行免疫电泳表明,这些抗血清特异性针对乙醇脱氢酶,并用于证明大鼠脑和肝脏的乙醇脱氢酶具有共同抗原。大鼠脑匀浆中乙醇脱氢酶的总活性通常相当低,其中高达10%的总活性归因于脑内所含血液中的活性;在严重肝损伤(通过四氯化碳实验诱导)的情况下,这一贡献可能高达60%。