Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:2.5.1.18 (
glutathione S-transferase
)
22,582
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Prostaglandin H-E isomerase (
EC 5.3.99.3
) was purified from human brain cytosol. Purification was by ammonium sulfate fractionation, diethylaminoethyl-Sepharose chromatography, gel filtration on a BioGel P-100 column, GSH-agarose chromatography, and MonoQ chromatography. The activity was eluted in two peaks from the MonoQ column, which were designated peaks 1 and 2. The molecular weights of peaks 1 and 2, determined by gel filtration, were 42,000 and 44,000, respectively. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis, peak 1 showed two bands at the molecular weights of 24,500 and 25,000, and peak 2 showed a single band at the molecular weight of 25,000, results suggesting that both were dimeric proteins. The pI values of both enzymes were approximately 5.4. The enzymes catalyzed selective conversion of prostaglandin H2 to prostaglandin E2. The Km values for prostaglandin H2 of peaks 1 and 2 were 147 and 308 microM, respectively, and the Vmax values were 380 and 720 nmol/min/mg of protein, respectively. GSH was required for the catalysis of both enzymes, and no other sulfhydryl compounds could support the reaction. A part of
glutathione S-transferase
(
EC 2.5.1.18
) was copurified with peaks 1 and 2 of
prostaglandin H-E isomerase
. Prostaglandin H-E isomerase activity of peak 2 enzyme was competitively inhibited by 1-chloro-2,4-dinitrobenzene, a substrate of
glutathione S-transferase
. These results suggested that prostaglandin H-E isomerases in human brain cytosol were identical with anionic forms of
glutathione S-transferase
.
...
PMID:Purification and properties of prostaglandin H-E isomerase from the cytosol of human brain: identification as anionic forms of glutathione S-transferase. 346 3
Exposure of NIH3T3 and pEJ serum-starved cells to platelet derived growth factor results in a 16 fold increase in the glutathione-dependent enzyme prostaglandin H2/prostaglandin E2 isomerase activity (
EC 5.3.99.3
). The response is rapid as a detectable increase in NIH3T3 cells occurs after only 7 minutes of exposure to the growth factor. Only a mild increase in another microsomal glutathione-dependent enzyme, microsomal glutathione transferase (
EC 2.5.1.18
), was detected after a 2 hour exposure to the growth factor.
...
PMID:PDGF-induces the glutathione-dependent enzyme PGH2/PGE2 isomerase in NIH3T3 and pEJ transformed fibroblasts. 829 33
