Lo H, Reeves R E
Mol Biochem Parasitol. 1980 Oct;2(1):23-30. doi: 10.1016/0166-6851(80)90045-6.
Amebal NADPH:flavin oxidoreductase was purified to apparent homogeneity. Molecular weights of 40 000 and 38 000 were estimated by gel filtration and by sodium dodecyl sulfate polyacrylamide gel electrophoresis, respectively, indicating that the enzyme is composed of a single polypeptide chain. The enzyme does not contain firmly bound flavin. It exhibited 20-fold selectivity for NADPH over NADH. With the former donor it reduced riboflavin, galactoflavin, FMN, or FAD. Aerobically the reducing equivalents were passed from reduced flavin to oxygen to form hydrogen peroxide. Intact amebae do not produce peroxide when they respire. If the title enzyme functions to reduce flavin in the intact cells some electron carrier must intervene between reduced flavin and oxygen so that the final step produces water instead of peroxide.
变形虫NADPH：黄素氧化还原酶被纯化至表观均一。通过凝胶过滤和十二烷基硫酸钠聚丙烯酰胺凝胶电泳分别估计其分子量为40000和38000，表明该酶由一条多肽链组成。该酶不含有紧密结合的黄素。它对NADPH的选择性比对NADH高20倍。以前者为供体时，它可还原核黄素、半乳糖黄素、FMN或FAD。在有氧条件下，还原当量从还原型黄素传递给氧以形成过氧化氢。完整的变形虫在呼吸时不产生过氧化物。如果标题酶在完整细胞中发挥还原黄素的作用，那么在还原型黄素和氧之间必须有某种电子载体介入，以便最终步骤产生水而不是过氧化物。
