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Titolo:
Glutathione S-transferases from rainbow trout liver and freshly isolated hepatocytes: purification and characterization
Autore:
Riol, MJM; Valinas, MCN; Fernandez, MAG; Lopez, MP;
Indirizzi:
Univ Santiago de Compostela, Fac Vet Med, Dept Toxicol, Lugo 27002, Spain Univ Santiago de Compostela Lugo Spain 27002 Toxicol, Lugo 27002, Spain
Titolo Testata:
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY C-TOXICOLOGY & PHARMACOLOGY
fascicolo: 2, volume: 128, anno: 2001,
pagine: 227 - 235
SICI:
1532-0456(200102)128:2<227:GSFRTL>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
METABOLIZING ENZYME-ACTIVITIES; CULTURED RAT HEPATOCYTES; SALMO-GAIRDNERI; INDUCTION; CYTOTOXICITY; FISH;
Keywords:
glutathione S-transferases; hepatocytes; liver; rainbow trout; isoenzymes;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Riol, MJM Univ Santiago de Compostela, Fac Vet Med, Dept Toxicol, Avda Madrid S-N, Lugo 27002, Spain Univ Santiago de Compostela Avda Madrid S-N Lugo Spain 27002 in
Citazione:
M.J.M. Riol et al., "Glutathione S-transferases from rainbow trout liver and freshly isolated hepatocytes: purification and characterization", COMP BIOC C, 128(2), 2001, pp. 227-235

Abstract

Glutathione S-transferases (GST) form an important family of biotransformation enzymes catalyzing the conjugation of glutathione to a great variety of xenobiotic compounds. The objective of this study was to compare the different characteristics of GST from freshly isolated rainbow trout hepatocytes with those corresponding to the total liver of the same fish, in order toestablish the similarities. GST was purified by affinity chromatography and enzymatic activity was determined towards two substrates, 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid (ETHA). The different isoenzymes were determined by HPLC associated with SDS-PAGE. Slight differences between the samples were obtained when the results corresponding to the enzyme activity were compared. HPLC results showed that all GST isoforms present in the total liver samples were represented in the isolated cells too, corresponding to isoforms with molecular masses of approximately 25.5 and 23.0 kDa. (C) 2001 EIsevier Science Inc. All rights reserved.

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Documento generato il 07/04/20 alle ore 22:42:25