Kinetic independence of the subunits of cytosolic glutathione transferase from the rat.

@article{Danielson1985KineticIO,
  title={Kinetic independence of the subunits of cytosolic glutathione transferase from the rat.},
  author={U Helena Danielson and Bengt Mannervik},
  journal={The Biochemical journal},
  year={1985},
  volume={231 2},
  pages={
          263-7
        }
}
The steady-state kinetics of the dimeric glutathione transferases deviate from Michaelis-Menten kinetics, but have hyperbolic binding isotherms for substrates and products of the enzymic reaction. The possibility of subunit interactions during catalysis as an explanation for the rate behaviour was investigated by use of rat isoenzymes composed of subunits 1, 2, 3 and 4, which have distinct substrate specificities. The kinetic parameter kcat./Km was determined with 1-chloro-2,4-dinitrobenzene, 4… CONTINUE READING

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