Purification, characterization and tissue distribution of human class theta glutathione S-transferase T1-1.
A high activity glutathione S-transferase T1-1 (GSTT1-1) towards dichloromethane was isolated from human liver cytosol and purified to homogenity in 18.5% yield with a purification factor of 4400-fold. The GSTT1-1 was also isolated from erythrocytes, but the enzyme activity decreased rapidly in the final stages of purification. The purified GSTT1-1-s were homo-dimeric enzymes with a subunit M1 value 25,300 and pI 6 64, as confirmed by SDS-PAGE, IEF and Western blot analysis. The N-terminal amino acid sequences of GSTT1-1 from liver and red blood cells, analyzed up to the 12th amino acid, were identical. Immunoblot analysis revealed that GSTT1-1 was also present in lung, kidney, brain, skeletal muscle, heart, small intestine and spleen, but not in lymphocytes.
Juronen
E
E
University of Tartu, Department of Human Biology and Genetics, Estonia.
Tasa
G
G
Uusküla
M
M
Pooga
M
M
Mikelsaar
A V
AV
D004912:Erythrocytes / Q000201:enzymology; D005982:Glutathione Transferase / Q000302:isolation & purification* / Q000493:pharmacokinetics*; D006801:Humans; D015151:Immunoblotting; D007525:Isoelectric Focusing; D008099:Liver / Q000201:enzymology*; D014018:Tissue Distribution
D005982:Glutathione Transferase