Reaction of liver alcohol dehydrogenase with halogenoacids. Fate of the iodide anion released by carboxymethylation and enzymic catalysis of iodide solvolysis.

@article{Biellmann1979ReactionOL,
  title={Reaction of liver alcohol dehydrogenase with halogenoacids. Fate of the iodide anion released by carboxymethylation and enzymic catalysis of iodide solvolysis.},
  author={Jean François Biellmann and Philippe Goulas and Jean Pierre Collin},
  journal={European journal of biochemistry},
  year={1979},
  volume={100 2},
  pages={461-5}
}
The fate of the iodide liberated during carboxymethylation of Cys-46 in horse liver alcohol dehydrogenase has been determined with 125I-labeled iodoacetate. The [125I]iodoacetic acid was prepared from mesyloxyacetic acid and sodium [125I]iodide. When carboxymethylation of the enzyme is carried out in solution or in the crystalline state, no iodide is bound to the protein. The rate of iodide during the reaction of iodoacetate, determined with an iodide-specific electrode, has been found to be… CONTINUE READING