Modification of Mouse Liver Glutathione S-Transferase Pi by Iodoacetic acid

1995 ◽  
Vol 23 (3) ◽  
pp. 485S-485S ◽  
Author(s):  
Sinéad B. Walsh ◽  
Timothy J. Mantle
Keyword(s):  
Mouse Liver ◽  
Iodoacetic Acid ◽  
Glutathione S Transferase ◽  
Liver Glutathione

Induction and development of mouse liver glutathione S-transferase activity

1981 ◽  
Vol 37 (5) ◽  
pp. 445-446 ◽  
Author(s):  
D. Dale Shoemaker ◽  
D. D. Dietrick ◽  
R. L. Cysyk
Keyword(s):  
Mouse Liver ◽  
Transferase Activity ◽  
Glutathione S Transferase ◽  
Liver Glutathione

scholarly journals Enantiotopic Selectivity in Monodemethylation of Fenitrothion by Rat Liver Glutathione S-Transferase Isoenzymes and Mouse Liver Cytosol

1994 ◽  
Vol 19 (4) ◽  
pp. 277-284 ◽  
Author(s):  
Koji WAKABAYASHI ◽  
Masanori HIZUE ◽  
Hiroshi NOZAKI ◽  
Mitsuru NAKAYAMA ◽  
Norio KURIHARA
Keyword(s):  
Rat Liver ◽  
Mouse Liver ◽  
Glutathione S Transferase ◽  
Liver Cytosol ◽  
Liver Glutathione

scholarly journals Protein depletion and refeeding change the proportion of mouse liver glutathione S-transferase subunits

1997 ◽  
Vol 1357 (3) ◽  
pp. 272-280 ◽  
Author(s):  
Rafael Garcı́a-Mata ◽  
Joël Capdevielle ◽  
Jean Claude Guillemot ◽  
Pascual Ferrara ◽  
Rubén D Conde ◽  
...  
Keyword(s):  
Mouse Liver ◽  
Glutathione S Transferase ◽  
Liver Glutathione ◽  
Protein Depletion

scholarly journals Inactivation of mouse liver glutathione S-transferase YfYf (Pi class) by ethacrynic acid and 5,5′-dithiobis-(2-nitrobenzoic acid)

1993 ◽  
Vol 294 (1) ◽  
pp. 57-62 ◽  
Author(s):  
M F Phillips ◽  
T J Mantle
Keyword(s):  
Mouse Liver ◽  
Ethacrynic Acid ◽  
Kinetic Studies ◽  
Cysteine Residue ◽  
Glutathione S Transferase ◽  
Acid Complex ◽  
Liver Glutathione ◽  
Nitrobenzoic Acid ◽  
Covalent Adduct ◽  
Acid Adduct

Mouse liver glutathione S-transferase YfYf (Pi class) reacts with [14C]ethacrynic acid to form a covalent adduct with a stoichiometry of 1 mol per mol of subunit. Proteolytic digestion of the enzyme-[14C]ethacrynic acid adduct with V8 protease produced an 11 kDa fragment containing radioactivity. Sequencing revealed this to be an N-terminal peptide (minus the first 15 residues, terminating at Glu-112) which contains only one cysteine residue (Cys-47). This is tentatively identified as the site of ethacrynic attachment. Kinetic studies reveal that glutathione S-conjugates protect against inactivation by ethacrynic acid, but the level of protection is not consistent with their potency as product inhibitors. A model is proposed in which glutathione S-conjugates and ethacrynic acid compete for the free enzyme, and a second molecule of ethacrynic acid reacts covalently with the enzyme-ethacrynic acid complex. The native protein contains one thiol reactive with 5,5′-dithiobis-(2-nitrobenzoic acid) at neutral pH. The resultant mixed disulphide, like the ethacrynic acid adduct, is inactive, but treatment with cyanide (which incorporates on a mol for mol basis) restores activity to 35% of that of the native enzyme.

Induction of mouse liver glutathione S-transferase by ethanol

1983 ◽  
Vol 32 (18) ◽  
pp. 2809-2811 ◽  
Author(s):  
Raymond M. David ◽  
Donald E. Nerland
Keyword(s):  
Mouse Liver ◽  
Glutathione S Transferase ◽  
Liver Glutathione
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