Description_x000D_ Application_x000D_ For Gel Filtration Chromatography_x000D_ Gel filtration molecular weight marker_x000D_ Biochem/physiol Actions_x000D_ ADH (alcohol dehydrogenase) is one of the first enzymes to be isolated and purified. NAD+ is its coenzyme. Three isozymes of yeast ADH, that is, yeast alcohol dehydrogenase-1, 2 and 3 (YADH-1, -2, -3) have been identified. YADH-1 is expressed during anaerobic fermentation, YADH-2 is expressed in the cytoplasm and YADH-3 is localized to the mitochondria. A 141kDa tetramer containing 4 equal subunits. The active site of each subunit contains a zinc atom. Each active site also contains 2 reactive sulfhydryl groups and a histidine residue._x000D_ Isoelectric point: 5.4-5.8_x000D_ Optimal pH: 8.6-9.0_x000D_ Substrates: Yeast ADH is most active with ethanol and its activity decreases as the size of the alcohol increases or decreases. Branched chain alcohols and secondary alcohols also have very low activity._x000D_ KM (ethanol) = 2.1 × 10-2 M_x000D_ KM (methanol = 1.3 × 10-1 M_x000D_ KM (isopropanol) = 1.4 × 10-1 M_x000D_ Inhibitors: Compounds that react with free sulfhydryls, including N-alkylmaleimides and iodoacetamide._x000D_ Zinc chelator inhibitors, including 1,10-phenanthroline,_x000D_ 8-hydroxyquinoline, 2,2′-dipyridyl, and thiourea._x000D_ Substrate analogue inhibitors, including β-NAD analogs, purine and pyrimidine derivatives, chloroethanol, and fluoroethanol._x000D_ Extinction Coefficient: E1% = 14.6 (water, 280 nm)