Purification of Aldose Reductase and Decolorization of Dye by the Enzyme
نویسنده
چکیده
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 and Mg 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.
منابع مشابه
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