Isolation, structural organization and mechanism of action of mitochondrial steroid hydroxylating systems

A scheme for the isolation of individual proteins of the 20S,22R-cholesterol hydroxylating system is presented. Physico-chemical and structural parameters of cytochrome P-450 are furnished. Self-reconstitution of indivudal proteins of the system into an enzyme unit is shown. Furthermore a regulation...

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Bibliographic Details
Published inActa biologica et medica Germanica Vol. 38; no. 2-3; p. 257
Main Authors Akhrem, A A, Lapko, V N, Lapko, A G, Shkumatov, V M, Chashchin, V L
Format Journal Article
LanguageEnglish
Published Germany 1979
Subjects
Adrenodoxin
Amino Acids - analysis
Animals
Cholesterol
Chromatography, Affinity
Cytochrome P-450 Enzyme System - isolation & purification
Electron Transport
Ferredoxin-NADP Reductase - isolation & purification
Mitochondria - enzymology
Molecular Weight
NADH, NADPH Oxidoreductases - isolation & purification
Steroid Hydroxylases - isolation & purification
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Summary:A scheme for the isolation of individual proteins of the 20S,22R-cholesterol hydroxylating system is presented. Physico-chemical and structural parameters of cytochrome P-450 are furnished. Self-reconstitution of indivudal proteins of the system into an enzyme unit is shown. Furthermore a regulation process of electron transport in the 20S,22R-cholesterol system is considered.
ISSN:0001-5318