Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S‐transferase π

@article{Ralat2003MonobromobimaneOA,
  title={Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S‐transferase π},
  author={L. Ralat and R. F. Colman},
  journal={Protein Science},
  year={2003},
  volume={12}
}
  • L. Ralat, R. F. Colman
  • Published 2003
  • Chemistry, Medicine
  • Protein Science
    • Monobromobimane (mBBr), functions as a substrate of porcine glutathione S‐transferase π (GST π): The enzyme catalyzes the reaction of mBBr with glutathione. S‐(Hydroxyethyl)bimane, a nonreactive analog of monobromobimane, acts as a competitive inhibitor with respect to mBBr as substrate but does not affect the reaction of GST π with another substrate, 1‐chloro‐2,4‐dinitrobenzene (CDNB). In the absence of glutathione, monobromobimane inactivates GST π at pH 7.0 and 25°C as assayed using mBBr as… CONTINUE READING
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    19 Citations
    Background Citations
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    Methods Citations
    2
    19 Citations
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