Shephard E A, Pike S F, Rabin B R, Phillips I R
Anal Biochem. 1983 Mar;129(2):430-3. doi: 10.1016/0003-2697(83)90573-0.
NADPH-cytochrome c (P-450) reductase from liver microsomes of phenobarbital-treated rats has been purified in a single step by affinity chromatography on agarose-hexane-adenosine 2',5'-diphosphate. As determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, enzyme assay, and radioimmunoassay the protein obtained by this single step procedure is as pure as that isolated by multicolumn procedures.
用琼脂糖-己烷-腺苷2',5'-二磷酸亲和层析一步法从苯巴比妥处理的大鼠肝脏微粒体中纯化出了NADPH-细胞色素c(P-450)还原酶。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳、酶活性测定和放射免疫测定确定,通过此一步法获得的蛋白质与通过多柱法分离得到的蛋白质纯度相同。