Apel K, Santel H J, Redlinger T E, Falk H
Eur J Biochem. 1980 Oct;111(1):251-8. doi: 10.1111/j.1432-1033.1980.tb06100.x.
The NADPH:protochlorophyllide oxidoreductase of barley has been solubilized from etioplast membranes and purified to apparent homogeneity. The highest specific activity measured for the purified enzyme was 1.6 nmol chlorophyllide formed (mg protein-1) per flash. Electrophoretic analysis of the purified enzyme on sodium dodecylsulfate/polyacrylamide gels revealed only one polypeptide of Mr 36000. Durig glycerol gradient centrifugation the enzyme migrates as a low-molecular-weight component. It is proposed that each enzyme molecule contains only one polypeptide chain. Assuming a molecular weight of 36000 for the enzyme, it was calculated that two or three protochlorophyllide molecules are bound to each enzyme molecule.
大麦的NADPH：原叶绿素酸酯氧化还原酶已从黄化质体膜中溶解出来并纯化至表观均一。纯化酶的最高比活性为每闪光形成1.6 nmol叶绿素酸酯（mg蛋白质-1）。在十二烷基硫酸钠/聚丙烯酰胺凝胶上对纯化酶进行电泳分析，仅显示一条分子量为36000的多肽。在甘油梯度离心中，该酶作为低分子量组分迁移。有人提出每个酶分子仅包含一条多肽链。假设该酶的分子量为36000，经计算每个酶分子结合两个或三个原叶绿素酸酯分子。
