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Titolo:
THE ENZYMOLOGY OF THE IN-VITRO OXIDATION OF PROLINTANE TO OXOPROLINTANE
Autore:
WHITTLESEA CMC; GORROD JW;
Indirizzi:
WELSH NATL SCH MED,WELSH CTR POST GRAD PHARMACEUT CARDIFF CF1 3XF WALES UNIV LONDON,KINGS COLL,CHELSEA DEPT PHARM LONDON SW3 6LX ENGLAND
Titolo Testata:
Journal of clinical pharmacy and therapeutics
fascicolo: 5, volume: 18, anno: 1993,
pagine: 357 - 364
SICI:
0269-4727(1993)18:5<357:TEOTIO>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENZYMATIC OXIDATION; METABOLISM; NICOTINE; CYTOCHROME-P-450; LIVER; ION; SYSTEMS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
31
Recensione:
Indirizzi per estratti:
Citazione:
C.M.C. Whittlesea e J.W. Gorrod, "THE ENZYMOLOGY OF THE IN-VITRO OXIDATION OF PROLINTANE TO OXOPROLINTANE", Journal of clinical pharmacy and therapeutics, 18(5), 1993, pp. 357-364

Abstract

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, 10000 g supernatant preparations. The results suggest that aldehyde oxidase is the soluble enzyme involved in oxoprolintane formation. Microsomal inhibitor studies showthat 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-450IIA, 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.

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Documento generato il 30/11/20 alle ore 16:35:15