The enzymology of the in–vitro oxidation of prolintane to oxoprolintane

Autor:	J. W. Gorrod, M. C. Whittlesea
Rok vydání:	1993
Předmět:	Pharmacology biology Cytochrome Stereochemistry Metabolite Potassium cyanide Cytochrome P450 Prolintane Monooxygenase chemistry.chemical_compound chemistry Biochemistry biology.protein medicine Microsome Pharmacology (medical) Aldehyde oxidase medicine.drug
Zdroj:	Journal of Clinical Pharmacy and Therapeutics. 18:357-364
ISSN:	1365-2710 0269-4727
DOI:	10.1111/j.1365-2710.1993.tb00603.x
Popis:	SUMMARY Studies to investigate the location of the enzymes responsible for oxoprolintane formation from prolintane, a sympathomimetic amine which is used to stimulate appetite, are reported. Aldehyde oxidase, cytochrome P–450 and flavin monooxygenase (FMO) inhibitors were used to investigate the process in male rabbit hepatic, 10 000g supernatant preparations. The results suggest that aldehyde oxidase is the soluble enzyme involved in oxoprolintane formation. Microsomal inhibitor studies show that cytochrome P–450, but not FMO, is also involved in prolintane metabolism to oxoprolintane. Results from animals pretreated with cytochrome P–450 inducers implicate cytochrome P–450UA, IIB and IIE in oxoprolintane formation but not the involvement of P–450IA. Experiments which incorporate potassium cyanide in the incubation medium with prolintane and hepatic preparations have led to the detection of a cyano adduct as a new metabolite. These results suggest that an iminium ion intermediate may be involved in oxoprolintane formation.
Databáze:	OpenAIRE
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