[醋酸钙不动杆菌中依赖NADP⁺的乙醇脱氢酶的纯化及各种性质]
[Purification and various properties of NADP+-dependent alcohol dehydrogenase from Acinetobacter calcoaceticus].
作者信息
Tauchert H, Grunow M, Harnisch H, Aurich H
出版信息
Acta Biol Med Ger. 1976;35(10):1267-72.
The constitutive NADP+-dependent alcohol dehydrogenase from Acinetobacter calcoaceticus can be accumulated about 50 fold in 3 purification steps. The end-product shows in the analytical polyacrylamide gel electrophoresis only one active enzyme band. The molecular weight of the enzyme was determined to be 235,000 by gel chromatography on Sephadex G 200, the smallest subunit shows a molecular weight of 61 000 on SDS electrophoresis. The isoelectric point is at 5.84. The KM values determined with primary aliphatic alcohols diminish in the range of the homologous order (C2--C10) with growing chain length. The KM value for hexanal is about 20 fold less than that for 1-hexanol.
来自醋酸钙不动杆菌的组成型烟酰胺腺嘌呤二核苷酸磷酸（NADP⁺）依赖性乙醇脱氢酶经过3步纯化可积累约50倍。在分析型聚丙烯酰胺凝胶电泳中，最终产物仅显示一条活性酶带。通过Sephadex G 200凝胶色谱法测定该酶的分子量为235,000，在十二烷基硫酸钠（SDS）电泳中最小亚基的分子量为61,000。其等电点为5.84。用伯脂肪醇测定的米氏常数（KM值）在同系物顺序（C2 - C10）范围内随链长增加而减小。己醛的KM值比1 - 己醇的约小20倍。
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