Solubilisation of D-amino acid dehydrogenase of Escherichia coli K12 and its re-binding to envelope preparations.
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.
D003605:D-Amino-Acid Oxidase / Q000302:isolation & purification*; D004926:Escherichia coli / Q000201:enzymology*; D008274:Magnesium / Q000494:pharmacology; D017830:Octoxynol; D011092:Polyethylene Glycols; D011550:Pseudomonas aeruginosa / Q000201:enzymology; D012995:Solubility
D011092:Polyethylene Glycols; D017830:Octoxynol; D003605:D-Amino-Acid Oxidase; D008274:Magnesium