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Titolo:
EXPRESSION AND INDUCTION OF ALL IMMUNOCHEMICALLY RELATED CLASS OF GLUTATHIONE S-TRANSFERASES IN DAPHNIA-MAGNA
Autore:
BALDWIN WS; LEBLANC GA;
Indirizzi:
N CAROLINA STATE UNIV,DEPT TOXICOL,BOX 7633 RALEIGH NC 27695 N CAROLINA STATE UNIV,DEPT TOXICOL RALEIGH NC 27695
Titolo Testata:
Comparative biochemistry and physiology. B. Comparative biochemistry
fascicolo: 2, volume: 113, anno: 1996,
pagine: 261 - 267
SICI:
0305-0491(1996)113:2<261:EAIOAI>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
DROSOPHILA; BINDING; TOXICITY; STRAINS; ACID;
Keywords:
ANTIBODIES; 1-CHLORO-2,4-DINITROBENZENE; DAPHNIA MAGNA; GLUTATHIONE S-TRANSFERASES; PHENOBARBITAL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
32
Recensione:
Indirizzi per estratti:
Citazione:
W.S. Baldwin e G.A. Leblanc, "EXPRESSION AND INDUCTION OF ALL IMMUNOCHEMICALLY RELATED CLASS OF GLUTATHIONE S-TRANSFERASES IN DAPHNIA-MAGNA", Comparative biochemistry and physiology. B. Comparative biochemistry, 113(2), 1996, pp. 261-267

Abstract

The cytosolic glutathione S-transferases (GSTs) are dimeric enzymes that are responsible for the conjugation of glutathione to an electrophilic center of a variety of lipophilic compounds. The purpose of the present study was to characterize the GSTs of Daphnia magna with respect to enzyme multiplicity, molecular weight, isoelectric points, and immunochemical distinction and to determine the inducibility of these enzymes by the prototypical mammalian GST inducer, phenobarbital. GSTs were purified from crude cystosols prepared. from daphnids by glutathione-sepharose affinity chromatography. SDS-polyacrylamide gel electrophoresis oi the affinity purified GSTs revealed the presence of multiplesubunits with molecular weights ranging from 26.9 to 30.2 kDa. Preparative electrofocusing separated GST activity into three major fractions having approximate isoelectric points of 4.5, 4.8 and 5.6. All of the catalytically active fractions contained a single protein band of the same molecular weight (30.2 kDa) during SDS-PAGE. A monoclonal antibody, prepared against the affinity-purified GST proteins, recognized three distinct proteins separated during analytical-scale isoelectric focusing (pI 4.6, 4.7 and 4.8). These proteins may represent a class ofGSTs distinct from the GST having a PI of 5.6. Treatment of daphnids with phenobarbital elevated both GST catalytic activity; and immunodefectable protein. These results demonstrate that multiple immunochemically related proteins of the same molecular weight but varying isoelectric points are responsible for most of the GST catalytic activity withthe substrate 1-chloro-2,4-dinitrobenzene.

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Documento generato il 05/07/20 alle ore 09:39:17