SHORT-TERM ADAPTATION OF HIGHER PLANTS TO CHANGING LIGHT INTENSITIES AND EVIDENCE FOR THE INVOLVEMENT OF PHOSPHORYLATION OF THE LIGHT HARVESTING CHLOROPHYLL alb PROTEIN COMPLEX OF PHOTOSYSTEM II

1984 ◽  
Vol 39 (6) ◽  
pp. 873-885
Author(s):  
Holger Dau ◽  
Ora Canaani
Keyword(s):  
Photosystem Ii ◽  
Protein Complex ◽  
Light Harvesting ◽  
Higher Plants ◽  
Short Term ◽  
Light Intensities ◽  
Short Term Adaptation ◽  
Changing Light

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.

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