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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Crankshaw D L, Hetnarski K, Wilkinson C F

Biochem J. 1979 Sep 1;181(3):593-605. doi: 10.1042/bj1810593.

NADPH-cytochrome c reductase was solubilized with bromelain and purified about 400-fold from sucrose/pyrophosphate-washed microsomal fractions from southern armyworm (Spodoptera eridania) larval midguts. 2. The enzyme has a mol.wt. of 70 035 +/- 1300 and contained 2 mol of flavin/mol of enzyme consisting of almost equimolar amounts of FMN and FAD. 3. Aerobic titration of the enzyme with NADPH caused the formation of a stable half-reduced state at 0.5 mol of NADPH/mol of flavin. 4. Kinetic analysis showed that the reduction of cytochrome c proceeded by a Bi Bi Ping Pong mechanism. 5. Apparent Km values for NADPH and cytochrome c and Ki values for NADP+ and 2'-AMP were considerably higher for the insect reductase than for the mammalian liver enzyme. 6. These are discussed in relation to possible differences in the active sites of the enzymes.

用菠萝蛋白酶溶解NADPH-细胞色素c还原酶，并从南方黏虫（草地贪夜蛾）幼虫中肠经蔗糖/焦磷酸洗涤的微粒体组分中纯化了约400倍。2. 该酶的分子量为70 035±1300，每摩尔酶含有2摩尔黄素，由几乎等摩尔量的FMN和FAD组成。3. 用NADPH对该酶进行需氧滴定，在每摩尔黄素0.5摩尔NADPH时形成稳定的半还原状态。4. 动力学分析表明，细胞色素c的还原通过双底物双产物乒乓机制进行。5. 昆虫还原酶对NADPH和细胞色素c的表观Km值以及对NADP+和2'-AMP的Ki值比哺乳动物肝脏酶的相应值高得多。6. 结合酶活性位点可能存在的差异对这些结果进行了讨论。

Crankshaw D L, Hetnarski K, Wilkinson C F

Biochem J. 1979 Sep 1;181(3):593-605. doi: 10.1042/bj1810593.

NADPH-cytochrome c reductase was solubilized with bromelain and purified about 400-fold from sucrose/pyrophosphate-washed microsomal fractions from southern armyworm (Spodoptera eridania) larval midguts. 2. The enzyme has a mol.wt. of 70 035 +/- 1300 and contained 2 mol of flavin/mol of enzyme consisting of almost equimolar amounts of FMN and FAD. 3. Aerobic titration of the enzyme with NADPH caused the formation of a stable half-reduced state at 0.5 mol of NADPH/mol of flavin. 4. Kinetic analysis showed that the reduction of cytochrome c proceeded by a Bi Bi Ping Pong mechanism. 5. Apparent Km values for NADPH and cytochrome c and Ki values for NADP+ and 2'-AMP were considerably higher for the insect reductase than for the mammalian liver enzyme. 6. These are discussed in relation to possible differences in the active sites of the enzymes.

用菠萝蛋白酶溶解NADPH-细胞色素c还原酶，并从南方黏虫（草地贪夜蛾）幼虫中肠经蔗糖/焦磷酸洗涤的微粒体组分中纯化了约400倍。2. 该酶的分子量为70 035±1300，每摩尔酶含有2摩尔黄素，由几乎等摩尔量的FMN和FAD组成。3. 用NADPH对该酶进行需氧滴定，在每摩尔黄素0.5摩尔NADPH时形成稳定的半还原状态。4. 动力学分析表明，细胞色素c的还原通过双底物双产物乒乓机制进行。5. 昆虫还原酶对NADPH和细胞色素c的表观Km值以及对NADP+和2'-AMP的Ki值比哺乳动物肝脏酶的相应值高得多。6. 结合酶活性位点可能存在的差异对这些结果进行了讨论。