P700 Chi-protein was isolated from a marine green alga Bryopsis corticulans with SDS-resolved thylakoid membranes by SDS-PAGE. After elution from the gel, the recovered protein revealed a 100 KD polypeptide by re-elec...P700 Chi-protein was isolated from a marine green alga Bryopsis corticulans with SDS-resolved thylakoid membranes by SDS-PAGE. After elution from the gel, the recovered protein revealed a 100 KD polypeptide by re-electrophoresis . The same SDS-PAGE procedure was used to isolate P700 Chl-proteins from spinach (Spinacea okracea ) and another marine green alga Codium fragile . Polyclonal antibodies to Bryopsis P700 protein were raised in rabbits. The antibodies were shown to cross-react with P700 Chl-protein and Chl-protein complexes containing P700 protein from B . Corticulans, C. f ragile, and even spinach. Results indicate similarity of the amino acid sequences of the P700 Chl-proteins and the highly conserved structure of the apoproteins of phylogenetically distant species over evolution. The antibodies cross-react with none of the components of PSUU in the species tested , indicating an independent pathway of evolution of photosystem I and photosystem II of later origin.展开更多
The excitation energy transfer from phycobiliproteins to thylakoid PSII of higher plants was investigated. When incubated with spinach thylakoids, phycobiliproteins isolated from red and blue- green algae transferred ...The excitation energy transfer from phycobiliproteins to thylakoid PSII of higher plants was investigated. When incubated with spinach thylakoids, phycobiliproteins isolated from red and blue- green algae transferred light energy absorbed to spinach PSII. The efficiency of energy transfer was dependent on the kind of phycobiliproteins used. If spinach thylakoids were replaced by the thylakoids of Brassica chinensis, R phycoerythin or C- phycocyanin did not transfer their excitation energy to PSII of Brassica chinensis unless allophycocyanin was present.展开更多
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...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展开更多
文摘P700 Chi-protein was isolated from a marine green alga Bryopsis corticulans with SDS-resolved thylakoid membranes by SDS-PAGE. After elution from the gel, the recovered protein revealed a 100 KD polypeptide by re-electrophoresis . The same SDS-PAGE procedure was used to isolate P700 Chl-proteins from spinach (Spinacea okracea ) and another marine green alga Codium fragile . Polyclonal antibodies to Bryopsis P700 protein were raised in rabbits. The antibodies were shown to cross-react with P700 Chl-protein and Chl-protein complexes containing P700 protein from B . Corticulans, C. f ragile, and even spinach. Results indicate similarity of the amino acid sequences of the P700 Chl-proteins and the highly conserved structure of the apoproteins of phylogenetically distant species over evolution. The antibodies cross-react with none of the components of PSUU in the species tested , indicating an independent pathway of evolution of photosystem I and photosystem II of later origin.
文摘The excitation energy transfer from phycobiliproteins to thylakoid PSII of higher plants was investigated. When incubated with spinach thylakoids, phycobiliproteins isolated from red and blue- green algae transferred light energy absorbed to spinach PSII. The efficiency of energy transfer was dependent on the kind of phycobiliproteins used. If spinach thylakoids were replaced by the thylakoids of Brassica chinensis, R phycoerythin or C- phycocyanin did not transfer their excitation energy to PSII of Brassica chinensis unless allophycocyanin was present.
基金Contribution No 1717 from the Institute of Oceanology, Academia Sinica,This subject was supported by the National Science Foundation of China.
文摘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
