Glutathione Transferases

Jakoby, William B.; Habig, William H.

doi:10.1016/b978-0-12-380002-2.50010-5

Cited by 203 publications

(89 citation statements)

References 109 publications

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“…Glutathione transferases (GST, EC 2.5.1.18) are a group of dimeric isoenzymes involved in the mechanism of detoxification from endogenous compounds and xenobiotics [1]. In addition they exhibit some binding properties towards different lipophilic compounds [2].…”

Section: Introductionmentioning

confidence: 99%

Identification of a highly reactive sulphydryl group in human placental glutathione transferase by a site‐directed fluorescent reagent

et al. 1990

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A fluorescent maleimide derivative, N-(4-anilino-l-naphthyl) maleimide (ANM), a specific probe for thiol groups, reacted with human placental glutathione transferase (GST, EC 2.5.1.18), causing a complete inactivation of the enzyme in a few minutes. The modified enzyme was denatured, alkylated and digested with (L-l-tosylamide-2-phenylethyl chloromethyl ketone)-trypsin. The tryptic digest was analysed by HPLC and a fluorescent peptide was obtained. The sequence of this peptide allowed us, by a comparison with a well known primary structure, to assign the position 47 to the most reactive cysteine of GST enzyme.

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Section: Introductionmentioning

confidence: 99%

Identification of a highly reactive sulphydryl group in human placental glutathione transferase by a site‐directed fluorescent reagent

et al. 1990

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“…Glutathione S-transferases (GST, EC 2.5.1.18) catalyze nucleophilic attack of glutathione on electrophilic centers in a wide variety of organic molecules [1,2]. The latter include xenobiotics as well as compounds endogenous to the organism.…”

Section: Introductionmentioning

confidence: 99%

Regulation of glutathione S‐transferase subunits 3 and 4 in cultured rat hepatocytes

et al. 1989

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mRNA levels of glutathione S-transferase (GST) subunits 3 and 4 were measured with a specific cDNA probe in adult rat hepatocytes maintained either in conventional culture or in coculture with rat liver epithelial cells. Four media conditions were used, i.e. with or without fetal calf serum (FCS) and with nicotinamide or dimethylsulfoxide (DMSO). When FCS was present in the culture medium, GST subunit 3 and 4 mRNAs were expressed at a level close to that found in freshly isolated hepatocytes during the whole culture period both in conventional culture and in coculture. All other culture conditions resulted in an increase of GST 3 and 4 mRNA levels. After exposure to phenobarbital an increase in GST 3 and 4 mRNA levels was demonstrated in both culture systems. Comparison with previous findings on the expression of GST subunits 1, 2 and 7 in the same culture conditions indicates that the different classes of GST are regulated independently.Glutathione S-transferase; Rat hepatocyte; Phenobarbital; (In vitro)

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“…This ability makes them important in the detoxication of endogenous and exogenous substances [I ,2]. Multiple forms of glutathione transferase exist in many species [2,3]. The cytosol fraction of mammalian liver contains isoenzymes with distinctly different properties.…”

Section: Introductionmentioning

confidence: 99%

“…Cytosotic glutathione transferases are dimeric proteins with subunit sizes of approx. 1M, 25000 [2].…”

Section: Introductionmentioning

confidence: 99%

Structural evidence for three different types of glutathione transferase in human tissues

1985

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Cytosolic glutathione transferase was purified from human placenta and human liver. Three different forms of the enzyme were obtained, the acidic (n). the near-neutral @), and the basic (CM) forms; two had free cc-amino groups (n, PI) and one had a blocked a-amino group (a-e). N-terminal sequence analyses and total compositions gave clearly different results for each form, although transferases IL and ,U showed 35% sequence homology in the N-terminal regions. with a l-residue shift in starting position. Consequently, the proteins are concluded to be products of three discrete but related genes. Glutat~zione transferee Amino acid sequence analysis H~an isoenzyme Sequence alignment ~-terminal processing dt~fere~ce~

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Glutathione Transferases

Cited by 203 publications

References 109 publications

Identification of a highly reactive sulphydryl group in human placental glutathione transferase by a site‐directed fluorescent reagent

Identification of a highly reactive sulphydryl group in human placental glutathione transferase by a site‐directed fluorescent reagent

Regulation of glutathione S‐transferase subunits 3 and 4 in cultured rat hepatocytes

Structural evidence for three different types of glutathione transferase in human tissues

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