Rosario Fernández M, Jörnvall H, Moreno A, Kaiser R, Parés X
Department of Biochemistry and Molecular Biology, Faculty of Sciences, Universitat Autònoma de Barcelona, Bellaterra, Spain.
FEBS Lett. 1993 Aug 16;328(3):235-8. doi: 10.1016/0014-5793(93)80934-m.
Octopus, squid and cuttle-fish organs were examined for alcohol dehydrogenase activity. Only one form was detectable, with properties typical of mammalian class III alcohol dehydrogenase. The corresponding protein was purified from octopus and enzymatically characterized. Ion-exchange and affinity chromatography produced a pure protein in excellent yield (73%) after 1600-fold purification. Enzymatic parameters with several substrates were similar to those for the human class III alcohol dehydrogenase, demonstrating a largely conserved function of the enzyme through wide lines of divergence covering vertebrates, cephalopods and bacteria. The results establish the universal occurrence of class III alcohol dehydrogenase and its strictly conserved functional properties in separate living forms. The absence of other alcohol dehydrogenases in cephalopods is compatible with the emergence of the ethanol-active class I type at a later stage, in lineages leading to vertebrates.
对章鱼、鱿鱼和乌贼的器官进行了乙醇脱氢酶活性检测。仅检测到一种形式，其特性为典型的哺乳动物Ⅲ类乙醇脱氢酶。从章鱼中纯化出了相应的蛋白质并对其进行了酶学特性分析。经过1600倍的纯化后，离子交换色谱和亲和色谱以极高的产率（73%）得到了纯蛋白。该酶对几种底物的酶学参数与人类Ⅲ类乙醇脱氢酶的相似，这表明在涵盖脊椎动物、头足类动物和细菌的广泛进化谱系中，该酶的功能在很大程度上是保守的。这些结果证实了Ⅲ类乙醇脱氢酶在不同生物形式中的普遍存在及其严格保守的功能特性。头足类动物中不存在其他乙醇脱氢酶，这与在导致脊椎动物的谱系中，乙醇活性Ⅰ类乙醇脱氢酶在后期出现的情况相符。
