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.
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Research Article| September 01 1974
Ribitol dehydrogenase from Klebsiella aerogenes. Purification and subunit structure
Susan S. Taylor;
Peter W. J. Rigby;
Biochem J (1974) 141 (3): 693–700.
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Susan S. Taylor, Peter W. J. Rigby, Brian S. Hartley; Ribitol dehydrogenase from Klebsiella aerogenes. Purification and subunit structure. Biochem J 1 September 1974; 141 (3): 693–700. doi: https://doi.org/10.1042/bj1410693
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