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1986 (1)
1Author    R. Steiner, A. A. Ngerhofer+, H. ScheerRequires cookie*
 Title    The Photosynthetic Apparatus of Ectothiorhodospira halochloris 2. Accessibility of the Membrane Polypeptides to Partial Proteolysis and Antenna Polypeptide Assignments to Specific Chromophores  
 Abstract    E. halochloris thylakoids and spheroplasts were treated with trypsin, thermolysin or proteinase K to determ ine which proteins are exposed at the different m embrane surfaces. B ased on SD S polyacrylamide analysis, all 9 polypeptides are exposed on the cytoplasm ic side. O nly one (28 k D a) is accessible from the periplasmic side. This polypeptide is generally isolated as the H-subunit o f the reaction centers of photosynthetic bacteria, but is in the case o f E. halochloris rather isolated with the antenna (B 800/1020) (Steiner and Scheer, Biochim . Biophys. A cta 807, 278, 1983). Proteolysis is accom panied by a shift of the absorption band at longest w avelengths from 1020 to 960 nm (B 800/960), which upon standing is shifted further to 680 nm ("B " 800/680). The spectral changes are similar to the ones reported earlier for treatm ent with acid, and are also inducible with urea. The correlation o f SD S-P A G E and absorption spectroscopy show s, that the chrom ophores absorbing at 1020 nm are transformed sim ultaneously with the degradation o f the 6.5 kD a (— a) polypeptide. 
  Reference    Z. Naturforsch. 41c, 571 (1986); received January 9 1986 
  Published    1986 
  Keywords    Bacterial Photosynthesis, Ectothiorhodospira, M embrane T opology, A ntenna Polypeptides, F luorescence, Circular D ichroism, Energy Transfer 
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 TEI-XML for    default:Reihe_C/41/ZNC-1986-41c-0571.pdf 
 Identifier    ZNC-1986-41c-0571 
 Volume    41