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- W2021482019 abstract "A rabbit antibody was prepared against a purified protease (bromelain)-solubilized fragment of NADPH-cytochrome c reductase from microsomes of southern armyworm (Spodoptera eridania) larval midguts. The antibody cross-reacted with the reductase from both control and pentamethylbenzene-induced midgut microsomes and inhibited the NADPH-dependent, but not the NADH-dependent, reduction of artificial electron acceptors. It also inhibited microsomal epoxidation, N-demethylation and O-demethylation, thus establishing NADPH-cytochrome c reductase as an obligatory component of the electron transport pathway leading to cytochrome P-450 in midgut microsomes. SDS-polyacrylamide gel electrophoresis of the immunoprecipitate obtained by treatment of deoxycholate-solubilized microsomes with the antibody indicated that the native reductase has a mol. wt. of 80,500. The antibody to the insect enzyme exhibited no cross-reactivity towards rat liver NADPH-cytochrome c reductase and an antibody prepared to the latter was similarly inactive towards the insect enzyme." @default.
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- W2021482019 date "1981-01-01" @default.
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- W2021482019 title "The functional role of nadph-cytochrome reductase in southern armyworm (Spodoptera eridania) midgut microsomes" @default.
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- W2021482019 doi "https://doi.org/10.1016/0020-1790(81)90019-6" @default.
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