Purification and characterization of two glutathione S-aryltransferase activities from rat liver.

@article{Askelf1975PurificationAC,
  title={Purification and characterization of two glutathione S-aryltransferase activities from rat liver.},
  author={P Askel{\"o}f and Claes Guthenberg and I Jakobson and Bengt Mannervik},
  journal={The Biochemical journal},
  year={1975},
  volume={147 3},
  pages={513-22}
}
Two forms of glutathione S-aryltransferase were purified from rat liver. The only differences noted between the two forms were in the chromatographic and electrophoretic properties, which permitted the separation of the two species. The molecular weights of the enzyme and its subunits were estimated as about 50000 and 23000 respectively. The steady-state kinetics did no follow Michaelis-Menten kinetics when one substrate concentration was kept constant while the second substrate concentration… CONTINUE READING

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Metabolic Conjugation andMetabolic Hydrolysis (Fishman

Biol. Chem
W. H., ed.), • 1970

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