Characterization of cytosolic glutathione S-transferases in California Halibut (Paralichthys californicus)

2007 ◽  
Vol 66 (2) ◽  
pp. 133-138 ◽  
Author(s):  
Rachel T. Donham ◽  
Andrea D. Luna ◽  
Sandra Chang ◽  
Dexter Morin ◽  
William T. Jewell ◽  
...  
Keyword(s):  
Paralichthys Californicus ◽  
California Halibut ◽  
Cytosolic Glutathione ◽  
Glutathione S Transferases

Characterization of cytosolic glutathione S-transferases in juvenile Chinook salmon (Oncorhynchus tshawytscha)

2005 ◽  
Vol 73 (3) ◽  
pp. 221-229 ◽  
Author(s):  
Rachel T. Donham ◽  
Dexter Morin ◽  
William T. Jewell ◽  
M.W. Lamé ◽  
H.J. Segall ◽  
...  
Keyword(s):  
Chinook Salmon ◽  
Oncorhynchus Tshawytscha ◽  
Juvenile Chinook Salmon ◽  
Cytosolic Glutathione ◽  
Glutathione S Transferases ◽  
Juvenile Chinook

scholarly journals Characterization of cytosolic glutathione-S- transferases (GSTs) involved in the metabolism of the aromatase inhibitor, Exemestane

2021 ◽  
pp. DMD-AR-2021-000635
Author(s):  
Irina Teslenko ◽  
Christy J.W. Watson ◽  
Zuping Xia ◽  
Gang Chen ◽  
Philip Lazarus
Keyword(s):  
Aromatase Inhibitor ◽  
Cytosolic Glutathione ◽  
Glutathione S Transferases

scholarly journals Characterization of methylation of rat liver cytosolic glutathione S-transferases by using reverse-phase h.p.l.c. and chromatofocusing

1990 ◽  
Vol 270 (2) ◽  
pp. 483-489 ◽  
Author(s):  
J A Johnson ◽  
T L Neal ◽  
J H Collins ◽  
F L Siegel
Keyword(s):  
Rat Liver ◽  
Time Course ◽  
Glutathione S Transferase ◽  
Reverse Phase ◽  
Cytosolic Glutathione ◽  
Glutathione S Transferases ◽  
Rat Liver Cytosol ◽  
Gst Activity

Glutathione S-transferase (GST) subunits in rat liver cytosol were separated by reverse-phase h.p.l.c.; five major proteins were isolated and identified as subunits 1, 2, 3, 4 and 8. F.p.l.c. chromatofocusing resolved the affinity-purified GST pool into nine different isoenzymes. The five basic (Alpha class) dimeric peaks of GST activity were 1-1, 1-2a, 1-2b, 2-2a and 2-2b. Reverse-phase h.p.l.c. analysis revealed that subunit 8 was also present in the protein peaks designated 1-1, 1-2a and 1-2b. The four neutral (Mu class) isoenzymes were 3-3, 3-4, 3-6 and 4-4. The GST pool was methylated in vitro before reverse-phase h.p.l.c. or f.p.l.c. chromatofocusing. Chromatofocusing indicated that the Mu class isoforms (3-3, 3-4 and 4-4) were the primary GSTs methylated, and h.p.l.c. analysis confirmed that subunits 3 and 4 were the major methyl-accepting GST subunits. The addition of calmodulin stimulated the methylation in vitro of GST isoenzymes 3-3, 3-4 and 4-4 by 3.0-, 7.5- and 9.9-fold respectively. Reverse-phase h.p.l.c. also indicated that only the methylation of GST subunits 3 and 4 was stimulated by calmodulin. Basic GST isoenzymes were minimally methylated and the methylation was not enhanced by calmodulin. Investigation of the time course of methylation of GST subunits 3 and 4 indicated that at incubation times less than 4 h the methylation of both Mu class subunits was stimulated by calmodulin, and that under such conditions subunit 4 was the preferred substrate. In contrast, there was essentially no calmodulin-stimulated methylation at incubation times of 4 or 6 h, and the methylation of subunit 3 was predominant. Kinetic parameters at 2 h of incubation were determined in the presence and in the absence of calmodulin. The addition of calmodulin doubled the Vmax. for methylation of both subunits 3 and 4 and decreased the Km of subunit 4 for S-adenosyl-L-methionine 3.6-fold. Finally, methylation was substoichiometric and after 6 h of incubation ranged from 2.8 to 7.6% on a mole-to-mole basis for subunits 4 and 3 respectively.

Characterization of cytosolic glutathione S-transferases in striped bass (Morone saxitilis)

2008 ◽  
Vol 69 (1) ◽  
pp. 58-63 ◽  
Author(s):  
Sandra Chang ◽  
Rachel T. Donham ◽  
Andrea D. Luna ◽  
Dexter Morin ◽  
William T. Jewell ◽  
...  
Keyword(s):  
Striped Bass ◽  
Cytosolic Glutathione ◽  
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

scholarly journals Novel functional association of rat testicular membrane-associated cytosolic glutathione S transferases and cyclooxygenase in vitro

2005 ◽  
Vol 7 (2) ◽  
pp. 171-178 ◽  
Author(s):  
S. Neeraja ◽  
B. Ramakrishna ◽  
A. S. Sreenath ◽  
G. V. Reddy ◽  
P. R. K. Reddy ◽  
...  
Keyword(s):  
Functional Association ◽  
Cytosolic Glutathione ◽  
Glutathione S Transferases

scholarly journals Mass spectrometric analysis of rat liver cytosolic glutathione S-transferases: modifications are limited to N-terminal processing

1995 ◽  
Vol 308 (1) ◽  
pp. 69-75 ◽  
Author(s):  
H I Yeh ◽  
C H Hsieh ◽  
L Y Wang ◽  
S P Tsai ◽  
H Y Hsu ◽  
...  
Keyword(s):  
Molecular Mass ◽  
Female Rats ◽  
Spectrometric Analysis ◽  
Affinity Column ◽  
Female Rat ◽  
Significant Difference ◽  
Cytosolic Glutathione ◽  
Glutathione S Transferases ◽  
Molecular Masses ◽  
Rat Livers

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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