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Polyc . lonal antibodies raised against LHC II isolated from SDS-solubilized Bryopsis corticulans thylakiod membranes by SDS-PAGE, were characterised by double immunodifiusion, Rocket immunoelectrophoresis and antigen-antibody crossed immunoelectro - phoresis assays showed the antibodies had strong cross-reaction with all B , corticulans LHC II components (even with those which were incubated in boiling water)and showed immunological cross-reactivity with LHC II polypeptides of spinach and the marine green alga Codium fragile. The results suggested that LHC II of different species had similar antigenic determinants and also conservation of amino acid sequences of the polypeptides during evolution, and that the antibodies could cross react with apoproteins of D2 proteins (which contain P680) from B. corticulans, spinach and C. fragile, but not with apoproteins of P 700 Chl-proteins. Our results indicated some similarities in primary structure between LHC II of different species, and between LHC II and D2
Polyc. Lonal antibodies raised against LHC II isolated from SDS-solubilized Bryopsis corticulans thylakiod membranes by SDS-PAGE, were characterized by double immunodifiusion, Rocket immunoelectrophoresis and antigen-antibody linked immunoelectro - phoresisctions showed the antibodies had strong cross-reaction with all B , corticulans LHC II components (even with those which were incubated in boiling water) and showed immunological cross-reactivity with LHC II polypeptides of spinach and the marine green alga Codium fragile. The results suggested that LHC II of different species had similar antigenic determinants and also conservations of amino acid sequences of the polypeptides during evolution, and that the antibodies could react with apoproteins of D2 proteins (which contain P680) from B. corticulans, spinach and C. fragile, but not with apoproteins of P 700 Chl-proteins Our results indicated some similarities in primary structure between LHC II of different species, and bet ween LHC II and D2