Ligand modification of corpus luteum mitochondrial cytochrome P-450 spectra and cholesterol monooxygenation: an assay of enzyme-specific inhibitors

Absorbance changes in the spectrum of cytochrome P-450 were related to the inhibition of [26-14C]cholesterol oxidation to [14C]isocaproate and pregnenolone in mitochondria from bovine corpus luteum produced by two types of ligands. Nitrogenous inhibitors, such as aminoglutethimide, elicit an absorpt...

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Veröffentlicht in:	Biochemistry (Easton) 1977-02, Vol.16 (4), p.593-600
Hauptverfasser:	Uzgiris, Vytautas I, Graves, Penelope E, Salhanick, Hilton A
Format:	Artikel
Sprache:	eng
Schlagworte:	Aminoglutethimide - pharmacology Animals Binding Sites Cattle Cholesterol - metabolism Corpus Luteum - enzymology Cytochrome P-450 Enzyme Inhibitors Cytochrome P-450 Enzyme System - metabolism Enzyme Inhibitors Female Kinetics Ligands Mitochondria - enzymology Oxygenases - antagonists & inhibitors Oxygenases - metabolism Pregnenes - pharmacology Pregnenolone - pharmacology Protein Binding Spectrophotometry
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