Isolation and protein chemical characterization of the B806-866 antenna complex of the green thermophilic bacterium Chloroflexus aurantiacus.
The B806-866 antenna complex was isolated from cytoplasmic membranes of the green thermophilic bacterium Chloroflexus aurantiacus. The membranes were treated with 7 M urea at 50 degrees C, the B806-866 antenna complex was solubilized with a mixture of Noni-fjdet P-40 (octylphenoxypolyethoxyethanol (Sigma)) and sodium dodecylsulphate (2:1) and isolated by sucrose density gradient centrifugation. This antenna complex was characterized by reversed-phase chromatography (fast polypeptide and polynucleotide liquid chromatography), amino acid and sequence analyses. The B806-866 antenna of Chloroflexus aurantiacus consists of two polypeptides: the B806-866-alpha and B806-866-beta polypeptides in an apparent stoichiometric ratio of 1:1, which may be equivalent to the structural elementary unit found in the antenna systems of many species of Rhodospirillaceae.
Wechsler
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Institut für Molekularbiologie und Biophysik, Zürich, Switzerland.
Brunisholz
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RA
Frank
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Zuber
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H
D000595:Amino Acid Sequence; D001419:Bacteria / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification*; D002850:Chromatography, Gel; D008969:Molecular Sequence Data; D045322:Photosynthetic Reaction Center Complex Proteins; D010860:Pigments, Biological / Q000737:chemistry / Q000302:isolation & purification*
D001426:Bacterial Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; D010860:Pigments, Biological; C069404:protein complex B806-866, Chloroflexus aurantiacus