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.
Publication types
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Alcohol Oxidoreductases / isolation & purification*
-
Amino Acid Sequence
-
Amino Acids / analysis
-
Chromatography, Gel
-
Chymotrypsin
-
Electrophoresis, Polyacrylamide Gel
-
Hydrogen-Ion Concentration
-
Iodoacetates
-
Kinetics
-
Klebsiella / enzymology*
-
Molecular Weight
-
Pepsin A
-
Ribose
-
Thermolysin
-
Trypsin
-
Ultracentrifugation
Substances
-
Amino Acids
-
Iodoacetates
-
Ribose
-
Alcohol Oxidoreductases
-
Chymotrypsin
-
Trypsin
-
Pepsin A
-
Thermolysin