Rat brain NADPH-dependent diaphorase. A possible relationship to cytochrome P450 reductase.

Abstract:

:An enzyme (NADPH-dependent diaphorase) present in rat brain microsomes has been solubilised and shown to utilise both nitrobluetetrazolium and cytochrome c as electron acceptors, when reduced by NADPH. The kinetics of the enzyme have been determined using cytochrome c (Km = 1.3 microM), NADPH (Km = 1.4 microM) and the Vmax (4.7 nmol/min/mg solubilised microsome protein). The subunit Mr is approximately 73,000 D and that of the native enzyme is 170,000-180,000 D, indicating that the enzyme is probably a dimer. Evidence is also provided to show that the enzyme is a flavoprotein, and that it has equimolar amounts of FAD and FMN with respect to the subunit concentration. It seems a possibility that the rat brain diaphorase enzyme may be cytochrome P450 reductase, EC 1.6.2.4.

journal_name

Biochem Pharmacol

journal_title

Biochemical pharmacology

authors

Kemp MC,Kuonen DR,Sutton A,Roberts PJ

doi

10.1016/0006-2952(88)90302-4

subject

Has Abstract

pub_date

1988-08-15 00:00:00

pages

3063-70

issue

16

eissn

0006-2952

issn

1873-2968

pii

0006-2952(88)90302-4

journal_volume

37

pub_type

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