A subfamily 2 homo-dimeric glutathione S-transferase mYrs-mYrs of class theta in mouse liver cytosol.
A homo-dimeric subfamily 2 glutathione (GSH) S-transferase (GST) mYrs-mYrs of the class theta was isolated from mouse liver cytosol and purified to homogeneity. The first 28 N-terminal amino acid sequence of the GST was completely identical to that of rat subfamily 2 GST Yrs-Yrs of the class theta. GST mYrs-mYrs cross-reacted with anti-rat GST Yrs-anti-sera but not with anti-sera raised against rat GSTs Ya-Ya (alpha), Yb1-Yb1 (mu), and Yp-Yp (pi) and represented more than 95% of the mouse liver cytosolic GST activity to scavenge the reactive sulfate ester 5-sulfoxymethylchrysene of the potent carcinogen 5-hydroxymethylchrysene. The mouse class theta GST had little activity toward 1-chloro-2,4-dinitrobenzene and was unretainable on GSH and an S-hexyl-GSH affinity columns. GST mYrs-mYrs had a much higher GSH peroxidase activity toward fatty acid hydroperoxides than did the other classes of mouse GSTs.
Hiratsuka
A
A
Department of Drug Metabolism and Molecular Toxicology, Tokyo University of Pharmacy and Life Science, School of Pharmacy, Japan.
Kanazawa
M
M
Nishiyama
T
T
Okuda
H
H
Ogura
K
K
Watabe
T
T
D000595:Amino Acid Sequence; D000818:Animals; D003600:Cytosol / Q000201:enzymology; D005979:Glutathione Peroxidase / Q000378:metabolism; D005982:Glutathione Transferase / Q000145:classification* / Q000235:genetics / Q000378:metabolism; D066298:In Vitro Techniques; D008099:Liver / Q000201:enzymology*; D008297:Male; D051379:Mice; D008969:Molecular Sequence Data; D011487:Protein Conformation; D051381:Rats; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D013379:Substrate Specificity; D014018:Tissue Distribution
D005979:Glutathione Peroxidase; D005982:Glutathione Transferase