Purification and Characterization of Two Glutathione S-Transferase Isozymes from Indica-Type Rice Involved in Herbicide Detoxification

2002 ◽  
Vol 72 (1) ◽  
pp. 10-23 ◽  
Author(s):  
Fan Deng ◽  
Kriton K. Hatzios
Keyword(s):  
Glutathione S Transferase ◽  
Purification And Characterization ◽  
Herbicide Detoxification

scholarly journals Purification and characterization of prostaglandin-H E-isomerase, a sigma-class glutathione S-transferase, from Ascaridia galli

1996 ◽  
Vol 313 (1) ◽  
pp. 223-227 ◽  
Author(s):  
David J. MEYER ◽  
Richmond MUIMO ◽  
Michael THOMAS ◽  
David COATES ◽  
R. Elwyn ISAAC
Keyword(s):  
Parasitic Nematode ◽  
Helminth Parasites ◽  
Ascaridia Galli ◽  
Glutathione S Transferase ◽  
Purification And Characterization ◽  
Parasitic Helminths ◽  
Accessory Cells ◽  
Glutathione S Transferases ◽  
Prostaglandin H

Comparison of partial primary sequences of sigma-class glutathione S-transferases (GSH) of parasitic helminths and a GSH-dependent prostaglandin (PG)-H D-isomerase of rat immune accessory cells suggested that some of the helminth enzymes may also be involved in PG biosynthesis [Meyer and Thomas (1995) Biochem. J. 311, 739-742]. A soluble GSH transferase of the parasitic nematode Ascaridia galli has now been purified which shows high activity and specificity in the GSH-dependent isomerization of PGH to PGE, comparable to that of the rat spleen enzyme in its isomerization of PGH to PGD, and similarly stimulates the activity of prostaglandin H synthase. The enzyme subunit is structurally related to the rat spleen enzyme and sigma-class GSH transferases of helminths according to the partial primary sequence. The data support the hypothesis that some sigma-class GSH transferases of helminth parasites are involved in PG biosynthesis which, in the case of PGE, is likely to be associated with the subversion or suppression of host immunity. A PG-H E-isomerase of comparable specificity and activity has not previously been isolated.

scholarly journals Differential induction of class Alpha glutathione S-transferases in mouse liver by the anticarcinogenic antioxidant butylated hydroxyanisole. Purification and characterization of glutathione S-transferase Ya1Ya1

1989 ◽  
Vol 263 (2) ◽  
pp. 393-402 ◽  
Author(s):  
L I McLellan ◽  
J D Hayes
Keyword(s):  
Female Mouse ◽  
Mouse Liver ◽  
Normal Mouse ◽  
Butylated Hydroxyanisole ◽  
Glutathione S Transferase ◽  
Purification And Characterization ◽  
Glutathione S Transferases ◽  
Differential Induction ◽  
Carcinogenic Compound

A novel cytosolic Alpha class glutathione S-transferase (GST) that is not normally expressed in mouse liver was found to be markedly induced (at least 20-fold) by the anti-carcinogenic compound butylated hydroxyanisole. This enzyme (designated GST Ya1 Ya1) did not bind to either the S-hexylglutathione-Sepharose or the glutathione-Sepharose affinity matrices, and purification was achieved by using bromosulphophthalein-glutathione-Sepharose. The purified isoenzyme, which comprises subunits of Mr 25,600, was characterized, and its catalytic, electrophoretic, immunochemical and structural properties are documented. GST Ya1 Ya1 was shown to be distinct from the Alpha class GST that is expressed in normal mouse liver and is composed of 25,800-Mr subunits; the Alpha class isoenzyme that is constitutively expressed in the liver is now designated GST Ya3 Ya3. Hepatic concentrations of GST Ya3 Ya3 were not significantly affected when mice were treated with butylated hydroxyanisole. Both Pi class GST (subunit Mr 24,800) and Mu class GST (subunit Mr 26,400) from female mouse liver were induced by dietary butylated hydroxyanisole. By contrast, hepatic concentrations of microsomal GST (subunit Mr 17,300) were unaffected.

scholarly journals Purification and characterization of human platelet glutathione-S- transferase

Blood ◽  
1986 ◽  
Vol 67 (6) ◽  
pp. 1595-1599
Author(s):  
J Loscalzo ◽  
J Freedman
Keyword(s):  
Specific Activity ◽  
Human Platelet ◽  
Reduced Glutathione ◽  
Human Platelets ◽  
Glutathione S Transferase ◽  
Purification And Characterization ◽  
Ph Optimum ◽  
Complete Purification ◽  
High Concentrations

A glutathione-S-transferase was isolated and purified to homogeneity from human platelets. With a combination of ammonium sulfate fractionation and chromatographic methods, 0.2 mg of pure enzyme was obtained from 9 X 10(11) platelets with a 12% recovery. The purified enzyme had a specific activity of 7.5 U per milligram, representing an approximately 1,100-fold purification. The enzyme was found to be anionic, with an isoelectric point of 4.6. With reduced glutathione as a co-substrate, platelet glutathione-S-transferase was most active with the synthetic substrate, 1-chloro-2,4-dinitrobenzene, less active with 1,2-dichloro-4-nitrobenzene, and essentially inactive with nitroglycerin and 1,2-epoxy-3-(p-nitrophenoxy)-propane. The pH optimum for activity with glutathione and 1-chloro-2,4-dinitrobenzene was 7.0. Indomethacin (1-(p-chlorobenzoyl)-5-methoxy-2-methyindole-3-acetic acid), a chlorobenzene derivative, noncompetitively inhibited human platelet glutathione-S-transferase with an apparent KI of 0.23 mmol/L. This study represents the first complete purification and characterization of a glutathione-S-transferase from platelets. The presence of this enzyme in the platelet, within which high concentrations of reduced glutathione coexist, suggests the potential importance of the platelet in detoxification reactions and in the synthesis of the glutathione adducts of leukotriene metabolism.

Sign in / Sign up

Export Citation Format

Share Document