Localization of periplasmic redox proteins of Alcaligenes faecalis by a modified general method for fractionating gram-negative bacteria.
A lysozyme-osmotic shock method is described for fractionation of Alcaligenes faecalis which uses glucose to adjust osmotic strength and multiple osmotic shocks. During phenylethylamine-dependent growth, aromatic amine dehydrogenase, azurin, and a single cytochrome c were localized in the periplasm. Their induction patterns are different from those for the related quinoprotein methylamine dehydrogenase and its associated redox proteins.
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Department of Biochemistry, The University of Mississippi Medical Center, Jackson, Mississippi 39216-4505, USA.
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Davidson
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D000421:Alcaligenes / Q000737:chemistry*; D001400:Azurin / Q000096:biosynthesis / Q000302:isolation & purification; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000302:isolation & purification*; D002458:Cell Fractionation / Q000379:methods*; D003574:Cytochrome c Group / Q000096:biosynthesis / Q000302:isolation & purification; D006090:Gram-Negative Bacteria / Q000737:chemistry*; D009113:Muramidase; D009997:Osmotic Pressure; D010084:Oxidation-Reduction; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000096:biosynthesis / Q000302:isolation & purification; D019897:Periplasm / Q000737:chemistry*; D013347:Subcellular Fractions / Q000737:chemistry
D001426:Bacterial Proteins; D003574:Cytochrome c Group; D001400:Azurin; C021567:methylamine dehydrogenase; D000587:Oxidoreductases Acting on CH-NH Group Donors; C037193:aromatic amine dehydrogenase; D009113:Muramidase