Mechanism of Action of Liver Alcohol Dehydrogenase

@article{Theorell1961MechanismOA,
  title={Mechanism of Action of Liver Alcohol Dehydrogenase},
  author={Hugo Theorell and J. M. McKee},
  journal={Nature},
  year={1961},
  volume={192},
  pages={47-50}
}
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At this Workshop, similar to the preceeding ones, much new information was presented and it was apparent how molecular biological techniques were influencing the direction of the research on the three families of enzymes discussed. Expand
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Kinetics of the inhibition of liver alcohol dehydrogenase by 1, lo-phenanthroline, and the effects of coenzyme and substrates thereon are examined and Mechanisms of action of this enzyme have been postulated based on the experimental findings. Expand
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DPN was determined under corresponding conditions, using as indicator the competition of DPNH and DPN for the same binding site(s) as well as the effects of formate and chloride, interfering with the kinetics particularly in acid solution. Expand
Complex formation of 1,10-phenanthroline with zinc ions and the zinc of alcohol dehydrogenase of horse liver.
TLDR
Spectrophotometry has been employed to determine and compare the stoichiometry of the interaction between OP and zinc ions and betweenOP and the enzyme, horse liver alcohol dehydrogenase, which has been shown to contain 2 g atoms of zinc per mole of protein. Expand
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