Brain mitochondrial cytochrome P-450scc: spectral and catalytic properties.

Abstract:

:The cytochrome P-450-dependent cholesterol side chain cleavage system of the brain has been studied using nonsynaptic mitochondria as the source of enzymatic activity. The system has been found to bind cholesterol and 11-deoxycorticosterone, producing type I difference spectra, whereas the binding of pregnenolone induced a reverse type I difference spectrum. Inhibitors of cytochrome P-450-linked monooxygenase activities produced type II spectra. The formation of labeled pregnenolone after incubation of brain mitochondria with [4-14C]cholesterol has been obtained, and this formation was inhibited by glutethimide, a specific inhibitor of cytochrome P-450scc. The functional significance of this enzymatic activity is discussed.

journal_name

Arch Biochem Biophys

authors

Walther B,Ghersi-Egea JF,Minn A,Siest G

doi

10.1016/0003-9861(87)90142-1

subject

Has Abstract

pub_date

1987-05-01 00:00:00

pages

592-6

issue

2

eissn

0003-9861

issn

1096-0384

pii

0003-9861(87)90142-1

journal_volume

254

pub_type

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