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Titolo:
PURIFICATION AND CHARACTERIZATION OF CYTOCHROME-P450 3A ENZYME FROM HEPATIC MICROSOMES OF UNTREATED DOGUERA BABOONS
Autore:
OHMORI S; KUDO S; NAKASA H; HORIE T; KITADA M;
Indirizzi:
CHIBA UNIV HOSP,FAC MED,DIV PHARM,CHUO KU,1-8-1 INOHANA CHIBA 260 JAPAN CHIBA UNIV,FAC PHARMACEUT SCI,CLIN PHARMACOL LAB,CHUO KU CHIBA 260 JAPAN EISAI & CO LTD TSUKUBA IBARAKI 30026 JAPAN
Titolo Testata:
Biological & pharmaceutical bulletin
fascicolo: 12, volume: 17, anno: 1994,
pagine: 1584 - 1588
SICI:
0918-6158(1994)17:12<1584:PACOC3>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
RAT-LIVER MICROSOMES; OXIDATIVE DRUG-METABOLISM; HUMAN-FETAL LIVERS; MOLECULAR-CLONING; GENETIC-POLYMORPHISM; CYNOMOLGUS MONKEYS; COMPLETE CDNA; SEQUENCE; FORMS; ISOZYMES;
Keywords:
CYTOCHROME P450; LIVER; MICROSOME; DOGUERA BABOON; TESTOSTERONE 6-BETA-HYDROXYLASE; ENZYME PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
49
Recensione:
Indirizzi per estratti:
Citazione:
S. Ohmori et al., "PURIFICATION AND CHARACTERIZATION OF CYTOCHROME-P450 3A ENZYME FROM HEPATIC MICROSOMES OF UNTREATED DOGUERA BABOONS", Biological & pharmaceutical bulletin, 17(12), 1994, pp. 1584-1588

Abstract

We isolated a form of cytochrome P450 (P450) from hepatic microsomes of untreated doguera baboons. The final preparation (referred to as P450 BLa) was apparently homogenous, as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The estimated minimum molecular weight of P450 BLa was 50 kDa. The N-terminal amino acid sequence of P450 BLa (identified 10 residues) was identical with that of P450 3A8 purified from cynomolgus monkeys. This protein was cross-reactive with antibodies raised against P450 3A4 and P450 CMLc which were P450 3A enzymes purified from hepatic microsomes of humans and cynomolgus monkeys, respectively. P450 BLa was capable of catalyzing testosterone 6 beta-hydroxylation and zonisamide reduction. P450 BLa antibody inhibited the activity of testosterone 6 beta-hydroxylase, but not the activitiesof testosterone 16 alpha- and 16 beta-hydroxylases in liver microsomes of doguera baboons. From these lines of evidence we conclude that P450 BLa can be classified as part of the P450 3A subfamily and acts as a constitutive testosterone 6 beta-hydroxylase in hepatic microsomes of doguera baboons.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 22:16:56