Brown A J, Lee C Y
Biochem J. 1979 Jun 1;179(3):479-82. doi: 10.1042/bj1790479.
A method for the purification of alcohol dehydrogenase from Drosophila melanogaster is described. The method makes use of 8-(6-aminohexyl)amino-5'-AMP, immobilized on Sepharose 4B, as an affinity ligand. Since alcohol dehydrogenase from Drosophila shows weak affinity for this column, a novel technique was developed to separate alcohol dehydrogenase from both unbound proteins and more strongly bound enzymes. The purification procedure is simple to operate and give a homogeneous preparation in good yield after only three steps.
描述了一种从黑腹果蝇中纯化乙醇脱氢酶的方法。该方法利用固定在琼脂糖4B上的8-(6-氨基己基)氨基-5'-AMP作为亲和配体。由于来自果蝇的乙醇脱氢酶对该柱的亲和力较弱,因此开发了一种新技术来从未结合的蛋白质和结合更强的酶中分离乙醇脱氢酶。纯化过程操作简单,仅经过三步就能以良好的产率得到均一的制剂。