title: Ribitol dehydrogenase from Klebsiella aerogenes. Purification and subunit structure.
abstract: Ribitol dehydrogenase has been purified to homogeneity from several strains of Klebsiella aerogenes. One strain yields 3-6g of pure enzyme from 1kg of cells. The enzyme is a tetramer of four subunits, mol.wt. 27000. Preliminary studies of the activity of the enzyme are reported. Peptide ;maps' together with the amino acid composition indicate that the subunits are identical.
mesh_terms: D000429:Alcohol Oxidoreductases / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002850:Chromatography, Gel; D002918:Chymotrypsin; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007461:Iodoacetates; D007700:Kinetics; D007709:Klebsiella / Q000201:enzymology*; D008970:Molecular Weight; D010434:Pepsin A; D012266:Ribose; D013820:Thermolysin; D014357:Trypsin; D014461:Ultracentrifugation
chemical_list: D000596:Amino Acids; D007461:Iodoacetates; D012266:Ribose; D000429:Alcohol Oxidoreductases; D002918:Chymotrypsin; D014357:Trypsin; D010434:Pepsin A; D013820:Thermolysin