Tsai C S, Al-Kassim L S, Mitton K P, Thompson L E, Van Es C, White J H
Comp Biochem Physiol B. 1987;87(1):79-85. doi: 10.1016/0305-0491(87)90473-1.
Alcohol dehydrogenases from various animal and plant sources were purified by a common procedure which employed DEAE, Sephadex-G100 and affinity chromatographies. The procedure achieves an 80-130 fold purification for animal enzymes. However, only a 5-15 fold purification for plant enzymes was attained because of the instability of these enzymes. Purified alcohol dehydrogenases from animal and plant sources differ in coenzyme and substrate specificities. The enzymes from mammalian, avian and fish livers display aldehyde oxidizing and esterolytic activities in addition to alcohol oxidizing activity. However, the enzymes from plants and yeast show only the oxidative activity toward alcohols. Chemical modifications have been performed to identify amino acid residues which are essential to the oxidative and esterolytic activities of alcohol dehydrogenases.
采用一种通用程序对来自各种动植物来源的乙醇脱氢酶进行纯化，该程序采用了二乙氨基乙基纤维素（DEAE）、葡聚糖凝胶G - 100和亲和色谱法。该程序可使动物酶纯化80至130倍。然而，由于这些植物酶的不稳定性，仅实现了5至15倍的纯化。来自动植物来源的纯化乙醇脱氢酶在辅酶和底物特异性方面存在差异。来自哺乳动物、鸟类和鱼类肝脏的酶除了具有醇氧化活性外，还表现出醛氧化和酯解活性。然而，来自植物和酵母的酶仅对醇具有氧化活性。已经进行了化学修饰以鉴定对乙醇脱氢酶的氧化和酯解活性至关重要的氨基酸残基。
