Purification, characterization and tissue distribution of human class theta glutathione s-transferase T1-1

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Abstract
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 Mt 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.

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