ArticleThe Biochemical journal1995
Mass spectrometric analysis of rat liver cytosolic glutathione S-transferases: modifications are limited to N-terminal processing.
Article in The Biochemical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- Changes in Glutathione Content in Liver Diseases: An Update.Antioxidants (Basel, Switzerland) · 2021Review
- Article
- Characterization and cloning of avian-hepatic glutathione S-transferases.The Biochemical journal · 1999Article
- Co-expression of glutathione S-transferase with methionine aminopeptidase: a system of producing enriched N-terminal processed proteins in Escherichia coli.The Biochemical journal · 1999Article
- Amino acid sequence of glutathione S-transferase rGSTM5* from rat testis.The Biochemical journal · 1998Article
- Characterization of chicken-liver glutathione S-transferase (GST) A1-1 and A2-2 isoenzymes and their site-directed mutants heterologously expressed in Escherichia coli: identification of Lys-15 and Ser-208 on cGSTA1-1 as residues interacting with ethacrynic acid.The Biochemical journal · 1997Article
- Quantitative profiling of tissue- and gender-related expression of glutathione S-transferase isoenzymes in the mouse.The Biochemical journal · 1997Article
- Mass spectrometric analysis of rat ovary and testis cytosolic glutathione S-transferases (GSTs): identification of a novel class-alpha GST, rGSTA6*, in rat testis.The Biochemical journal · 1997Article
- Conformational stability of pGEX-expressed Schistosoma japonicum glutathione S-transferase: a detoxification enzyme and fusion-protein affinity tag.Protein science : a publication of the Protein Society · 1997Article
- Characterization of pig liver glutathione S-transferases using HPLC-electrospray-ionization mass spectrometry.The Biochemical journal · 1996Article
- Rat kidney glutathione S-transferase 1 subunits have C-terminal truncations.The Biochemical journal · 1996Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cytosolic glutathione S-transferases (GSTs) from rat livers were purified using an S-hexylglutathione affinity column. The GST subunits were resolved by reverse-phase HPLC and their molecular masses were determined by electrospray mass spectrometry. The major hepatic GSTs detected were subunits 1, 1', 2, 3 and 4, with molecular mass of 25,520, 25,473, 25,188, 25,782 and 25,571 Da respectively. Subunits 6, 7 and 10 are minor components, with molecular mass of 25,551, 23,308 and 25,211 Da respectively. Alternatively, the hepatic GSTs were purified using a glutathione affinity column. Subunits 1, 1', 2, 8 and 10 were eluted from this column with GSSG, the oxidized form of glutathione. Subunit 8 has a molecular mass of 25,553 Da. The remaining proteins on the glutathione affinity column were removed with glutathione and S-hexylglutathione. Subunits 2, 3, 4 and 6 could be detected in the eluate. We could not detect any significant difference in molecular mass between GSTs isolated from male and female rat livers. Cytosolic GSTs were isolated from livers of buthionine sulphoximine-treated female rats for MS analysis. The molecular masses obtained were identical to those determined for the controls.
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