The liver monooxygenase system of Brazilian freshwater fish

dc.contributor.authorLeitao, MAS
dc.contributor.authorAffonso, E. G.
dc.contributor.authorSilva, MFE da
dc.contributor.authorMeirelles, N. C.
dc.contributor.authorRantin, F. T.
dc.contributor.authorVercesi, A. E.
dc.contributor.authorJunqueira, VCB
dc.contributor.authorDegterev, I. A.
dc.contributor.institutionUniversidade Federal de São Carlos (UFSCar)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionRussian Acad Sci
dc.description.abstractContent of cytochromes b(5) and P-450, and activities of NADPH-cytochrome c (P-450) reductase (NCR) and 7-ethoxyresorufin O-deethylase (EROD) were measured in liver microsomes prepared from two South American endemic fish, Brycon cephalus and Colossoma macropomum, from tilapia, Oreochromis niloticus, and from Swiss mice, Mus musculus. which served as a control. Strong hemoglobin binding to fish liver microsomal membranes (FLM) altered visible spectra of microsomal cytochromes. Consequently, special precautions during FLM preparation, including liver perfusion followed by repeated washing of microsomes, were required in the study of microsomal cytochromes from these fish. FLM from all fish studied here had a significantly lower content of microsomal cytochromes but a similar level of NCR and EROD activities compared to mouse liver microsomes (MLM). Strong response of the monooxygenase system in O. niloticus to water pollution was detected with both specific cytochrome P-450 content and EROD activity increasing sharply. the optical spectra of hemoglobin from B. cephalus and C. macropomum were analyzed and some differences in shape and relative extinction were observed compared to known hemoglobins. (C) 2000 Elsevier Science Inc. All lights reserved.en
dc.description.affiliationUniv Fed Sao Carlos, Dept Physiol Sci, BR-13565905 Sao Carlos, SP, Brazil
dc.description.affiliationUniv São Paulo, Dept Biochem, São Paulo, SP, Brazil
dc.description.affiliationState Univ Campinas, UNICAMP, Fac Med Sci, Inst Biol,Dept Biochem, Campinas, SP, Brazil
dc.description.affiliationState Univ Campinas, UNICAMP, Fac Med Sci, Dept Clin Pathol, Campinas, SP, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Med, São Paulo, SP, Brazil
dc.description.affiliationRussian Acad Sci, Inst Biochem Phys, Moscow, Russia
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Med, São Paulo, SP, Brazil
dc.description.sourceWeb of Science
dc.identifier.citationComparative Biochemistry and Physiology C-pharmacology Toxicology & Endocrinology. Oxford: Pergamon-Elsevier B.V., v. 126, n. 1, p. 29-38, 2000.
dc.publisherElsevier B.V.
dc.relation.ispartofComparative Biochemistry and Physiology C-pharmacology Toxicology & Endocrinology
dc.rightsAcesso restrito
dc.subjectcytochrome P-450en
dc.subjectcytochrome b(5)en
dc.subjectliver microsomesen
dc.subjectneotropical fishen
dc.subjectNCR activityen
dc.titleThe liver monooxygenase system of Brazilian freshwater fishen