Ribitol dehydrogenase from Klebsiella aerogenes. Purification and subunit structure.
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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.
SUBMITTER: Taylor SS
PROVIDER: S-EPMC1168174 | biostudies-other | 1974 Sep
REPOSITORIES: biostudies-other
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