PURIFICATION OF HUMAN AND RAT-KIDNEY ALDOSE REDUCTASE

In the present study we report on a rapid two-step affinity chromatogr aphic procedure to purify aldose reductase from human and rat kidney p apilla and inner medulla. This enzyme, which is responsible for sorbit ol formation in the kidney, was purified 145-fold from rat and 76-fold from human kidneys by consecutive Blue Sepharose and Matrex Orange ch romatography. SDS-PAGE showed a single band of 38 kD for the human enz yme and a doublet of similar molecular weight for the rat kidney aldos e reductase. The enzyme was characterized by substrate specificity and kinetic constants found identical to that of other organs purified pr eviously.