Aldose and aldehyde reductases in human tissues.
Immunochemical characterizations of aldose reductase and aldehyde reductases I and II, partially purified by DEAE-cellulose (DE-52) column chromatography from human tissues, were carried out by immunotitration, using antisera raised against the homogenous preparations of human and bovine lens aldose reductase and human placenta aldehyde reductase I and aldehyde reductase II. Anti-aldose antiserum cross-reacted with aldehyde reductase I, anti-aldehyde reductase I antiserum cross-reacted with aldose reductase and anti-aldehyde reductase II antiserum precipitated aldehyde reductase II, but did not cross-react with aldose reductase or aldehyde reductase I from all the tissues examined. DE-52 elution profiles, substrate specificity and immunochemical characterization indicate that aldose reductase is present in human aorta, brain, erythrocyte and muscle; aldehyde reductase I is present in human kidney, liver and placenta; and aldehyde reductase II is present in human brain, erythrocyte, kidney, liver, lung and placenta. Monospecific anti-alpha and anti-beta antisera were purified from placenta anti-aldehyde reductase I antiserum, using immunoaffinity techniques. Anti-alpha antiserum precipitated both aldehyde reductase I and aldose reductase, whereas anti-beta antibodies cross-reacted with only aldehyde reductase I. Based on these studies, a three gene loci model is proposed to explain the genetic interrelationships among these enzymes. Aldose reductase is a monomer of alpha subunits, aldehyde reductase I is a dimer of alpha and beta subunits and aldehyde reductase II is a monomer of delta subunits.
D000445:Aldehyde Oxidoreductases / Q000276:immunology / Q000378:metabolism*; D000449:Aldehyde Reductase / Q000276:immunology / Q000378:metabolism*; D005260:Female; D006801:Humans; D013401:Sugar Alcohol Dehydrogenases / Q000378:metabolism*; D014018:Tissue Distribution
D013401:Sugar Alcohol Dehydrogenases; D000449:Aldehyde Reductase; D000445:Aldehyde Oxidoreductases