Solubilisation of D-amino acid dehydrogenase of Escherichia coli K12 and its re-binding to envelope preparations |
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Authors: | H Jones W A Venables |
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Institution: | Microbiology Department, University College, Newport Road, Cardiff CF2 1TA, Gt. Britain |
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Abstract: | D-amino acid dehydrogenase was found to be solubilised from envelope preparations of Escherichia coli by treatment with detergents but not with aqueous buffer solutions. Triton X-100-solubilised dehydrogenase was found to rebind to envelope preparations from the wild strain (AB 259) and its D-amino acid dehydrogenase-less mutant (DAD 13), and activities higher than those of native envelopes could be obtained. Re-binding was stimulated by magnesium. D-alanine stimulated cytochrome reduction and oxygen uptake were reconstituted when the solubilised dehydrogenase rebound to AB 259 envelopes. Re-binding of solubilised dehydrogenase to DAD 13 envelopes was independent of the growth medium used for DAD 13. |
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Keywords: | déshydrogénase solubilisation liaison oxydase dehydrogenase solubilisation re-binding oxidase |
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