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1996 (1)
1Author    Grzegorz JackowskiRequires cookie*
 Title    The Subcomplex Organization of the Major Chlorophyll «/6-Protein Light- Harvesting Complex of Photosystem II (LHCII) in Barley Thylakoid Membrane  
 Abstract    The major chlorophyll «/b-protein light-harvesting complex o f photosystem II (LHCII) isolated form barley photosynthetic membrane was shown to contain five major polypeptides only two o f which (26.7 and 25.6 kDa) were found to be its true constituents as judged by the ability to migrate as oligomers in various analytical systems. When analyzed by a vertical-bed non-denaturing isoelectric focusing the LHCII was resolved into five trimeric subcom­ plexes (designated 1 -5 in order of decreasing p i) containing either only 26.7 kDa polypep­ tide (subcom plexes 1 and 2) or 26.7 and 25.6 kDa ones associated at 2:1 ratio (subcom plexes 3 -5) . The polypeptide of 26.7 kDa could be split by denaturing isoelectric focusing into fifteen molecular forms while nine molecular species were found to be constituents of 25.6 kDa polypeptide. The subcom plexes 1 -5 contained molecular forms of one or both polypep­ tides associated in sets of 7 -9 . Our findings favour the view that the apoproteins of LHCII are much more heterogenous than thought before. 
  Reference    Z. Naturforsch. 51c, 454 (1996); received November 23 1995/March 4 1996 
  Published    1996 
  Keywords    Barley, Isoelectric Focusing Light Harvesting Complex Polypeptide Subcomplex, Trimer 
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 TEI-XML for    default:Reihe_C/51/ZNC-1996-51c-0454.pdf 
 Identifier    ZNC-1996-51c-0454 
 Volume    51