Meso-2,3-dimercaptosuccinic acid increases the inhibition of glutathione S-transferase activity from rat liver cytosol supernatants by di-n-butyltin dichloride

1985 ◽  
Vol 57 (1) ◽  
pp. 67-68 ◽  
Author(s):  
Gerhard Hennighausen ◽  
Jutta Merkord
Keyword(s):  
Rat Liver ◽  
Dimercaptosuccinic Acid ◽  
Transferase Activity ◽  
Glutathione S Transferase ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

scholarly journals A study of the structures of the YaYa and YaYc glutathione S-transferases from rat liver cytosol Evidence that the Ya monomer is responsible for lithocholate-binding activity

1981 ◽  
Vol 197 (2) ◽  
pp. 491-502 ◽  
Author(s):  
J D Hayes ◽  
R C Strange ◽  
I W Percy-Robb
Keyword(s):  
Rat Liver ◽  
Lithocholic Acid ◽  
Binding Activity ◽  
Glutathione S Transferase ◽  
Liver Cytosol ◽  
Molecular Weights ◽  
Tryptic Digest ◽  
Glutathione S Transferases ◽  
Limited Digestion ◽  
Rat Liver Cytosol

The two dimeric lithocholic acid-binding proteins previously identified as ligandin (YaYa) and glutathione S-transferase B (YaYc) were isolated from rat liver cytosol. These proteins have molecular weights of 44000 and 47000 respectively. The recovery of these two proteins from liver was not affected by the addition of the proteinase inhibitor Trasylol. No spontaneous interconversion between these two proteins was observed on storage. YaYa and YaYc proteins yielded peptides of identical molecular weight after limited digestion with Staphylococcus aureus V8 proteinase. Analytical and preparative tryptic-digest peptide ‘maps’ showed that all the soluble peptides obtained from YaYa protein were also recovered from YaYc protein. Approximately six extra soluble peptides, which were not recovered from YaYa protein, were obtained from the tryptic digest of YaYc protein. Subdigests of the insoluble tryptic-digest ‘cores’ also resulted in the recovery of identical peptides from both proteins. Evidence is presented that the Ya subunit possessed by both proteins is identical; glutathione S transferase B is a hybrid of ligandin and glutathione S-transferase AA. The Ya monomer is responsible for lithocholate binding.

scholarly journals Cholic acid binding by glutathione S-transferases from rat liver cytosol

1980 ◽  
Vol 185 (1) ◽  
pp. 83-87 ◽  
Author(s):  
J D Hayes ◽  
R C Strange ◽  
I W Percy-Robb
Keyword(s):  
Bile Acid ◽  
Cholic Acid ◽  
Reduced Glutathione ◽  
Binding Activity ◽  
Transferase Activity ◽  
Glutathione S Transferase ◽  
Liver Cytosol ◽  
Glutathione S Transferases ◽  
Rat Livers ◽  
Rat Liver Cytosol

Cholic acid-binding activity in cytosol from rat livers appears to be mainly associated with enzymes having glutathione S-transferase activity; at least four of the enzymes in this group can bind the bile acid. Examination of the subunit compositions of different glutathione S-transferases indicated that cholic acid binding and the ability to conjugate reduced glutathione with 1,2-dichloro-4-nitrobenzene may be ascribed to different subunits.

scholarly journals Carbon Tetrachloride-Induced Alteration of Glutathione S-Transferase in Rat Liver Cytosol and Plasma

1989 ◽  
Vol 6 (3) ◽  
pp. 175-185 ◽  
Author(s):  
Fumio FUKAI ◽  
Sachiko NISHIZAWA ◽  
Masae KURANO ◽  
Kumiko TANIGUCHI ◽  
Takashi KATAYAMA
Keyword(s):  
Carbon Tetrachloride ◽  
Rat Liver ◽  
Glutathione S Transferase ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

scholarly journals Identification of two lithocholic acid-binding proteins. Separation of ligandin from glutathione S-transferase B

1979 ◽  
Vol 181 (3) ◽  
pp. 699-708 ◽  
Author(s):  
J D Hayes ◽  
R C Strange ◽  
I W Percy-Robb
Keyword(s):  
Enzyme Activity ◽  
Binding Proteins ◽  
Peptide Mapping ◽  
Lithocholic Acid ◽  
Transferase Activity ◽  
Glutathione S Transferase ◽  
Liver Cytosol ◽  
Structural Differences ◽  
Distinct Subunit ◽  
Rat Liver Cytosol

1. Two lithocholic acid-binding proteins in rat liver cytosol, previously shown to have glutathione S-transferase activity, were resolved by CM-Sephadex chromatography. 2. Phenobarbitone administration resulted in induction of both binding proteins. 3. The two proteins had distinct subunit compositions indicating that they are dimers with mol.wts. 44 000 and 47 000. 4. The two lithocholic acid-binding proteins were identified by comparing their elution volumes from CM-Sephadex with those of purified ligandin and glutathione S-transferase B prepared by published procedures. Ligandin and glutathione S-transferase B were eluted separately, as single peaks of enzyme activity, at volumes equivalent to the two lithocholic acid-binding proteins. 5. Peptide ‘mapping’ revealed structural differences between the two proteins.

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