Purification and characterization of human-brain aldose reductase.

@article{Wermuth1982PurificationAC,
  title={Purification and characterization of human-brain aldose reductase.},
  author={Bendicht Wermuth and H B{\"u}rgisser and Kurt M. Bohren and J P. von Wartburg},
  journal={European journal of biochemistry},
  year={1982},
  volume={127 2},
  pages={279-84}
}
Aldose reductase (EC 1.1.1.21) from human brain has been purified to apparent homogeneity. The enzyme catalyzes the NADPH-dependent reduction of several physiological and xenobiotic aldehydes. Isocorticosteroids, e.g. isocortisol and isocorticosterone, are the best substrates (Km less than 1 micron), followed by aromatic and arylalkyladehydes, including biogenic aldehydes (Km = 3 - 15 microM). The activity towards aldoses is highest with glyceraldehyde (Km = 25 microM) and decreases with… CONTINUE READING
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