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Application of electron‐donor properties of glucose oxidase and xanthine oxidase for reduction of microsomal NAD(P)H‐dependent electron‐transport chains
Author(s) -
Izotov MV,
Shcherbakov VM,
Spiridonova SM,
Devichenskiy VM,
Benediktova SA
Publication year - 1991
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1991.tb00144.x
Subject(s) - microsome , xanthine oxidase , chemistry , xanthine dehydrogenase , dithionite , biochemistry , oxidase test , electron transport chain , nad+ kinase , cytochrome , enzyme
The reduction of cytochromes b5 and P‐450 in mammalian hepatic microsomes by glucose oxidase and xanthine oxidase has been investigated. Under anaerobic conditions cytochrome b5 is reduced by glucose oxidase to the “dithionite” level, while cytochrome P‐450 remains oxidized. Under the same conditions xanthine oxidase completely reduces both hemoproteins. Besides, neither glucose oxidase nor xanthine oxidase reduces isolated cytochromes. They can be reduced only after addition of microsomes to incubation media. Only in this case are the cytochromes, both isolated and included in microsomal membranes, reduced. The participation of microsomal flavoproteins in the reduction reaction is discussed. The method suggested makes it possible to substantially decrease the rates of reduction of microsomal hemoproteins, thus permitting the investigation of interactions between microsomal NADH‐ and NADPH‐dependent electron‐transport chains and electron carriers.