Characterization of rat cornea aldehyde dehydrogenase.

@article{Evces1989CharacterizationOR,
  title={Characterization of rat cornea aldehyde dehydrogenase.},
  author={S Evces and Ronald Lindahl},
  journal={Archives of biochemistry and biophysics},
  year={1989},
  volume={274 2},
  pages={
          518-24
        }
}
  • S Evces, Ronald Lindahl
  • Published in
    Archives of biochemistry and…
    1989
  • Chemistry, Medicine
  • Aldehyde dehydrogenase has been purified from rat cornea in a single step. The enzyme is a class 3 aldehyde dehydrogenase. Cornea aldehyde dehydrogenase is a 100-kDa dimer composed of 51-kDa subunits, prefers NADP+ as coenzyme, and preferentially oxidizes benzaldehyde-like aromatic aldehydes as well as medium chain length (4-9 carbons) aliphatic aldehydes. The substrate and coenzyme specificity, immunochemical properties, effect of disulfiram, pH profile, and isoelectric point of cornea… CONTINUE READING

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