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1996[X]
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 
2Author    Grzegorz JackowskiRequires cookie*
 Title    Senescence-Related Changes in the Subcomplex Arrangement of the Major Light-Harvesting Chlorophyll a/b-Protein Complex of Photosystem II (LHCII) as Influenced by Cytokinin  
 Abstract    The major light-harvesting chlorophyll a /b -protein complex of photosystem II (LHCII) from fresh barley leaves could be resolved by non-denaturing IEF into five trimeric subcom­ plexes designated 1 -5 in order of decrasing pi value. IEF-based analysis of PSII particles isolated from leaves in which the processes of senescence were induced by detachement and dark-incubation in the presence of water for 0 -8 days let us reveal that substantial rearrangements of LHCII organization took place throughout the course of senescence com ­ prising a step-wise decline in relative abundance of subcom plexes 1 -3 (down to 0-58% of the initial abundance during 8 days of aging) and an increase in the relative abundance of the subcom plexes 4 and 5. Using SDS-PAGE and immunoblot analysis it was shown that the rearrangements were linked to the changes in the relative levels of LHCII apoproteins i.e. 26.7 and 25.6 kDa ones. The changes comprised the preferential disappearance of the 26.7 kDa polypeptide and an enrichment of 25.6 kD a one and most probably reflect the hetero­ geneity among LHCII apoproteins concerning their stability under the conditions of chi loss. Kinetin was able to repress the senescence-related rearrangements in LHCII subcomplex organization at late stages of aging (5 -8 days) by preventing over this time period the disap­ pearance of 26.7 kD a polypeptide and the enrichement of 25.6 kDa one. 
  Reference    Z. Naturforsch. 51c, 464 (1996); received Novem ber 23 1995/ 
  Published    1996 
  Keywords    Aging, Barley, Isoelectric Focusing, Polypeptide, Rearrangement 
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 DEBUG INFO      
 TEI-XML for    default:Reihe_C/51/ZNC-1996-51c-0464.pdf 
 Identifier    ZNC-1996-51c-0464 
 Volume    51