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Purification of Aldose Reductase and Decolorization of Dye by the Enzyme

  • Jang, Mi (Department of Chemistry, Myongji University) ;
  • Kim, Kyung-Soon (Department of Chemistry, Myongji University)
  • Published : 2009.12.31

Abstract

Aldose reductase was purified to electrophoretic homogeneity from porcine liver. The purified enzyme was a monomer of 36 kDa. The enzyme was strongly inhibited by $Cu^{2+}\;and\;Mg^{2+}$ ions. Incubation of the enzyme with pyridoxal 5'-phosphate led to complete inhibition of enzymatic activity, suggesting that lysine residue is involved at or near the active site of the enzyme. The enzyme exhibited a broad substrate specificity. Furthermore, the enzyme was capable of decolorizing Alizarin, an anthraquinone dye.

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