The reconstitution of a Photosystem II protein complex, P-700-chlorophyll a-protein complex and light-harvesting chlorophyll ab-protein

1982 ◽  
Vol 679 (3) ◽  
pp. 410-421 ◽  
Author(s):  
A.W.D. Larkum ◽  
Jan M. Anderson
Keyword(s):  
Photosystem Ii ◽  
Chlorophyll A ◽  
Protein Complex ◽  
Light Harvesting

The Oligomeric Arrangement of the Light-Harvesting Chlorophyll a/6-Protein Complex of Photosystem II

1994 ◽  
Vol 49 (5-6) ◽  
pp. 337-342 ◽  
Author(s):  
Grzegorz Jackowski ◽  
Ewa Kluck
Keyword(s):  
Photosystem Ii ◽  
Chlorophyll A ◽  
Protein Complex ◽  
Light Harvesting ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Dianthus Caryophyllus ◽  
Lhc Ii ◽  
Induced Aggregation ◽  
Oligomeric Forms

Abstract The light-harvesting chlorophyll a/b-protein complex of photosystem II (LHC II) was isolated from carnation (Dianthus caryophyllus L.) leaves by K+-induced aggregation of n-hep-tylthioglucoside-treated photosystem II particles. When solubilized with a mixture of lithium docedyl sulphate, octyl-β-D-glucopyranoside and dodecyl-β-D-maltoside the LHC II was re­ solved by mild sodium dodecyl sulphate-polyacrylamide gel electrophoresis into four oligo­meric forms and a monomeric one. LHC II contained five major polypeptides only two of which (27 and 26 kDa) were found to be its authentic components. The oligomeric forms of LHC II were found to differ in the stoichiometric ratios of the polypeptides present. The 26 kD a polypeptide was enriched in the largest oligomeric forms while the 27 kDa polypep­tide tended to form a monomer or to assemble as lower oligomeric states of LHC II.

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

1996 ◽  
Vol 51 (7-8) ◽  
pp. 464-472 ◽  
Author(s):  
Grzegorz Jackowski
Keyword(s):  
Photosystem Ii ◽  
Chlorophyll A ◽  
Relative Abundance ◽  
Protein Complex ◽  
Light Harvesting ◽  
Immunoblot Analysis ◽  
Time Period ◽  
Sds Page ◽  
Barley Leaves ◽  
Late Stages

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 subcomplexes 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 comprising a step-wise decline in relative abundance of subcomplexes 1 -3 (down to 0-58% of the initial abundance during 8 days of aging) and an increase in the relative abundance of the subcomplexes 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 disappearance of 26.7 kD a polypeptide and the enrichement of 25.6 kDa one.

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