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An acid glutathione S-transferase (EC: 2.5.1.18) from human lung was purified and characterized. The purification procedure included two isoelectric focusing runs, Sephadex G-100 gel filtration, glutathione-affinity chromatography, and Sephadex G-75 gel filtration. With respect to the properties studied the acid lung transferase differed from human liver transferases alpha-epsilon, but it bore a close resemblance to the other human low pI transferases. Bilirubin affected the kinetics of the lung enzyme markedly differently as compared with transferase p, suggesting possible nonidentity between these enzymes. The acid lung transferase represented about 97% of the total glutathione transferase activity of the lung 100,000 g supernatant used in this work.
K Koskelo, and
E Valmet, and
R Tenhunen
June 1986,
Blood,
K Koskelo, and
E Valmet, and
R Tenhunen
March 1991,
The Biochemical journal,
K Koskelo, and
E Valmet, and
R Tenhunen
January 1979,
Acta chemica Scandinavica. Series B: Organic chemistry and biochemistry,
K Koskelo, and
E Valmet, and
R Tenhunen
December 1983,
The Biochemical journal,
K Koskelo, and
E Valmet, and
R Tenhunen
January 2009,
Artificial cells, blood substitutes, and immobilization biotechnology,
K Koskelo, and
E Valmet, and
R Tenhunen
March 1983,
Biochemistry,
K Koskelo, and
E Valmet, and
R Tenhunen
January 1984,
Lung,
K Koskelo, and
E Valmet, and
R Tenhunen
December 1984,
Biochemical and biophysical research communications,
K Koskelo, and
E Valmet, and
R Tenhunen
January 2005,
Polish journal of microbiology,
K Koskelo, and
E Valmet, and
R Tenhunen
January 1996,
Archives of toxicology,
