Abstract
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.
Publication types
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Comparative Study
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Alcaligenes / chemistry*
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Azurin / biosynthesis
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Azurin / isolation & purification
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Bacterial Proteins / biosynthesis
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Bacterial Proteins / isolation & purification*
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Cell Fractionation / methods*
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Cytochrome c Group / biosynthesis
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Cytochrome c Group / isolation & purification
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Gram-Negative Bacteria / chemistry*
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Muramidase
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Osmotic Pressure
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Oxidation-Reduction
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Oxidoreductases Acting on CH-NH Group Donors / biosynthesis
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Oxidoreductases Acting on CH-NH Group Donors / isolation & purification
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Periplasm / chemistry*
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Subcellular Fractions / chemistry
Substances
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Bacterial Proteins
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Cytochrome c Group
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Azurin
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methylamine dehydrogenase
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Oxidoreductases Acting on CH-NH Group Donors
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aromatic amine dehydrogenase
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Muramidase