Nakanisi N, Kobayashi H, Yamada S
Comp Biochem Physiol B. 1984;78(3):515-8. doi: 10.1016/0305-0491(84)90089-0.
NADH-specific dihydropteridine reductase [EC 1.6.99.7] was purified from mouse mastocytoma P-815 cells. Km values for NADH and NADPH were determined to be 1.4 microM and 32 microM, respectively, using tetrahydro-6-methylpterin. Molecular weight was 50,000, and subunit molecular weight was 25,000. The enzymes from P-815 and liver of host mouse (DBA/2) showed similar electrophoretic mobility on polyacrylamide gel. The P-815 enzyme reacted with antiserum against bovine liver NADH-specific dihydropteridine reductase, forming a single precipitin line.
从小鼠肥大细胞瘤P - 815细胞中纯化出了NADH特异性二氢蝶啶还原酶[EC 1.6.99.7]。使用四氢-6-甲基蝶呤测定NADH和NADPH的Km值分别为1.4微摩尔和32微摩尔。分子量为50,000,亚基分子量为25,000。来自P - 815细胞和宿主小鼠(DBA/2)肝脏的酶在聚丙烯酰胺凝胶上显示出相似的电泳迁移率。P - 815酶与抗牛肝NADH特异性二氢蝶啶还原酶的抗血清反应,形成一条单一的沉淀线。