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1988 (1)
1Author    Matthias Kuhn, Andreas Thiel, Peter BögerRequires cookie*
 Title    The 9-kDa Phosphoprotein Involved in Photoinhibition  
 Abstract    Photosystem-II particles exhibit strong photoinhibition. Short-term illumination of photosys-tem-II particles with high-intensity light (5000 piE/m 2 x s) leads to a typical change of the protein pattern on SDS-PAGE. Two proteins are mainly affected, namely the well-described 32-kDa herbicide-binding protein which probably is degraded [1] and, first published here, the 9-kDa phosphoprotein, whose function in the PS-II complex is still unknown. This protein is not de-graded, but seems to be linked to other polypeptides of the PS-II complex. During light treatment new bands of 23, 41, 50 and 54 kDa appear in the protein pattern of SDS-PAGE. A monospecific antiserum was produced against the 9-kDa phosphoprotein to investigate its fate. After light treatment the antibodies reacted with new proteins of higher molecular weights, most pronounced with a 23-kDa and a 41-kDa peptide. 
  Reference    Z. Naturforsch. 43c, 413—417 (1988); received February 15 1988 
  Published    1988 
  Keywords    9-kDa Phosphoprotein, Photosystem-II Particles, Photoinhibition, Protein Phosphorylation, Antibody 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0413.pdf 
 Identifier    ZNC-1988-43c-0413 
 Volume    43