The binding of sulfonamides to horse liver alcohol dehydrogenase.

@article{Western1984TheBO,
  title={The binding of sulfonamides to horse liver alcohol dehydrogenase.},
  author={A. Western and C. Syvertsen and J. McKinley-McKee},
  journal={Biochemical pharmacology},
  year={1984},
  volume={33 5},
  pages={
          731-8
        }
}
The binding of sulfonamides to the active site of horse liver alcohol dehydrogenase has been studied by their effect on affinity labelling and steady state kinetics. Affinity labelling with iodoacetate and BIP has been used to study binding to free enzyme. The unsubstituted sulfonamide, sulfanilamide (I), shows very weak binding compared to the other sulfonamides tested. Most important for binding is the type of substituent attached to the parent sulfonamide, particularly when as in… Expand

References

SHOWING 1-10 OF 23 REFERENCES
Ionization-linked cooperative interactions in the active site of horse liver alcohol dehydrogenase.
The imidazole-promoted inactivation of horse-liver alcohol dehydrogenase.
Anion-binding to liver alcohol dehydrogenase, studied by rate of alkylation.
Combination of bovine carbonic anhydrase with a fluorescent sulfonamide.
Anion binding to liver alcohol dehydrogenase.
Effects of pH and inhibitors on some properties related to metal binding in bovine carbonic anhydrase.
  • S. Lindskog
  • Medicine, Chemistry
  • The Journal of biological chemistry
  • 1963
Chemical reactions of sulfonamides with carbonic anhydrase.
  • J. Coleman
  • Chemistry, Medicine
  • Annual review of pharmacology
  • 1975
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2
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