Characterization of glutathione S-transferases from day-old chick livers

Biochemistry ◽  
1990 ◽  
Vol 29 (3) ◽  
pp. 744-750 ◽  
Author(s):  
Li Hsueh Chang ◽  
Liu Fen Chuang ◽  
Chueh Ping Tsai ◽  
Chen Pei D. Tu ◽  
Ming F. Tam
Keyword(s):  
Glutathione S Transferases

Purification and characterization of glutathione S-transferases in human retina

1984 ◽  
Vol 3 (11) ◽  
pp. 1273-1280 ◽  
Author(s):  
Shivendra V. Singh ◽  
Dat D. Dao ◽  
Satish K. Srivastava ◽  
Yogesh C. Awasthi
Keyword(s):  
Human Retina ◽  
Purification And Characterization ◽  
Glutathione S Transferases

Characterization of two μ class glutathione S-transferases from guinea pig lens

2000 ◽  
Vol 32 (1) ◽  
pp. 99-104 ◽  
Author(s):  
Naoto Noda ◽  
Hideki Adachi ◽  
Hirofumi Nanjo ◽  
Tomoyuki Terada
Keyword(s):  
Guinea Pig ◽  
Glutathione S Transferases

scholarly journals Cloning and characterization of two glutathione S-transferases from pyrethroid-resistant Culex pipiens

2012 ◽  
Vol 68 (5) ◽  
pp. 764-772 ◽  
Author(s):  
Aman I Samra ◽  
Shizuo G Kamita ◽  
Hong-Wei Yao ◽  
Anthony J Cornel ◽  
Bruce D Hammock
Keyword(s):  
Culex Pipiens ◽  
Glutathione S Transferases

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 Characterization of glutathione S-transferases in rat kidney. Alteration of composition by cis-platinum

1988 ◽  
Vol 252 (1) ◽  
pp. 127-136 ◽  
Author(s):  
G M Trakshel ◽  
M D Maines
Keyword(s):  
Specific Activity ◽  
Rat Kidney ◽  
Male Rats ◽  
Glutathione S Transferase ◽  
Aberrant Form ◽  
Glutathione S Transferases ◽  
Exchange Matrix ◽  
Rat Kidney Cytosol

We have developed chromatographic and mathematical protocols that allowed the high resolution of glutathione S-transferase (GST) subunits, and the identification of a previously unresolved GST monomer in rat kidney cytosol; the monomer was identified tentatively as subunit 6. Also, an aberrant form of GST 7-7 dimer appeared to be present in the kidney. This development was utilized to illustrate the response of rat kidney GST following cis-platinum treatment in vivo. Rat kidney cytosol was separated into three ‘affinity families’ of GST activity after elution from a GSH-agarose matrix. The affinity peaks were characterized by quantitative differences in their subunit and dimeric compositions as determined by subsequent chromatography on a cation-exchange matrix and specific activity towards substrates. By use of these criteria, the major GST dimers of affinity peaks were tentatively identified. The major GST dimers in peak I were GST 1-1 and 1-2, in affinity peak II it was GST 2-2, and in peak III they were GST 3-3 and 7-7. GST 3-6 and/or 4-6, which have not been previously resolved in kidney cytosol, were also present in peak II. Alterations in the kidney cytosolic GST composition of male rats were detected subsequent to the administration of cis-platinum (7.0 mg/kg subcutaneously, 6 days). This treatment caused a pronounced alteration in the GST profile, and the pattern of alteration was markedly different from that reported for other chemicals in the kidney or in the liver. In general, the cellular contents of the GSTs of the Alpha and the Mu classes decreased and increased respectively. It is postulated that the decrease in the Alpha class of GSTs by cis-platinum treatment may be related to renal cortical damage and the loss of GSTs in the urine. The increase in the Mu class of GSTs could potentially stem from a lowered serum concentration of testosterone; the latter is a known effect of cis-platinum treatment.

Glutathione S-transferases of lung: purification and characterization of human lung glutathione S-transferases

Lung ◽  
1984 ◽  
Vol 162 (1) ◽  
pp. 27-36 ◽  
Author(s):  
Catherine A. Partridge ◽  
Dat D. Dao ◽  
Yogesh C. Awasthi
Keyword(s):  
Human Lung ◽  
Purification And Characterization ◽  
Glutathione S Transferases

Purification and characterization of glutathione S-transferases of rat uterus

1996 ◽  
Vol 28 (11) ◽  
pp. 1271-1283 ◽  
Author(s):  
Sharad S. Singhal ◽  
C. Yallampalli ◽  
Jyotsana Singhal ◽  
John T. Piper ◽  
Sanjay Awasthi
Keyword(s):  
Purification And Characterization ◽  
Rat Uterus ◽  
Glutathione S Transferases

scholarly journals Purification and Biochemical Characterization of Glutathione S-Transferases inBactrocera minax(Diptera: Tephritidae)

2012 ◽  
Vol 95 (3) ◽  
pp. 593-601 ◽  
Author(s):  
Er-Hu Chen ◽  
Wei Dou ◽  
Fei Hu ◽  
Song Tang ◽  
Zhi-Mo Zhao ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Glutathione S Transferases
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