Nine pigment-protein complexes were separated and characterized from intact Chroomonasplacoidea chloroplasts by IEF. The bands Ⅰ-Ⅵ with their isoelectric points （pI） values from 4 to 6 were phycocyanin components;...Nine pigment-protein complexes were separated and characterized from intact Chroomonasplacoidea chloroplasts by IEF. The bands Ⅰ-Ⅵ with their isoelectric points （pI） values from 4 to 6 were phycocyanin components; bands Ⅷ and Ⅸ （pI = 2.8-3.6） were chlorophyll-protein complexes. According to absorption and fluorescence spectra, band VII was designated as a novel phycocyanin-Chla/c2-protein complex （pI ≈ 3.4-3.7）. These results indicated that phycocyanin is structurally and functionally coupled with chlorophyll-protein complex in C. placoidea, and probably interacted with electrostatic force in combination.展开更多
An active photosystem(PS)Ⅱparticle and two light-harvesting complexes,as well as their subcomplexes that have not been reported previously,were isolated from a cryptophyte Chroomonas placoidea by Triton X-100 sucrose...An active photosystem(PS)Ⅱparticle and two light-harvesting complexes,as well as their subcomplexes that have not been reported previously,were isolated from a cryptophyte Chroomonas placoidea by Triton X-100 sucrose density gradient centrifugation.The fluorescence spectra revealed that there were efficient energy couplings between phycocyanin(PC645)and chlorophyll(Chl)within both zonesⅢandⅣof the gradient,which were designated respectively as light-harvesting complex and PSⅡparticles whose size was 15-20 nm according to negative staining in electron microscopy.When the two complexes were further resolved into sub-complexes,the energy coupling was retained in the core PSⅡcomplex(named as zoneⅣ-2 of the sucrose gradient),which contained almost no outer antenna pigment Chl c.Sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE)showed that the PC645 components appeared in Chl-containing protein complexes were mainly the β subunit with molecular weight of 20 kDa.These results demonstrate that PC645 in this cryptophyte was structurally but preferentially combined with the light-harvesting complex and PSⅡcore.The excitation energy absorbed by PC645 could be directly transferred to Chl a(especially the long wavelength of Chl a)in the PSⅡreaction center or via the Chl a/c-protein complex.The β subunit corresponded to the terminal fl uorescence emission and might play an important role in transmitting energy from PC645 to the Chl-protein complex.The results will help in elucidating the architecture and function of the energy transfer system comprising phycobiliproteins and Chl-protein complexes in cryptophytes.展开更多
A new phycocyanin（PC） fluorescent subunit namedβ_2（18kDa） was isolated and characterized by both SDS-PAGE and isoelectric focusing（IEF） from a species of cryptophytic alga Chroomonas placoidea.PC was separated ...A new phycocyanin（PC） fluorescent subunit namedβ_2（18kDa） was isolated and characterized by both SDS-PAGE and isoelectric focusing（IEF） from a species of cryptophytic alga Chroomonas placoidea.PC was separated and purified by ammonium sulfate sedimentation followed by two steps of Sephadex G-100 chromatography.After denatured in 4 mol/L urea for 48 h,PC was divided into two fractions by passing through a Sephacryl S-100 chromatography column twice.The blue fraction（S-1） containedβsubunits with a maximal absorbance at 595 nm in visible light region.While the green fraction（S-2） enriched inαsubunits showed a characteristic long wavelength absorbance at 680-700 nm region and exhibited a relatively low molecular weight of 9.4（α_1） and 8.5 kDa（α_2）.Fraction S-1 also consisted of two different fluorescent subunits with molecular weight of 20.1 kDa（β_1） and 18 kDa （β_2） and differed from each other on isoelectric points of pH 5.7（ft） and 6.0（ft）,respectively.Further investigation of peptide sequence will help a lot in elucidating the new subunit ft that was smaller in size and more neutral than the known ft subunit,and may provide an alternative explanation in structure of cryptophytic phycobiliproteins.展开更多
文摘Nine pigment-protein complexes were separated and characterized from intact Chroomonasplacoidea chloroplasts by IEF. The bands Ⅰ-Ⅵ with their isoelectric points （pI） values from 4 to 6 were phycocyanin components; bands Ⅷ and Ⅸ （pI = 2.8-3.6） were chlorophyll-protein complexes. According to absorption and fluorescence spectra, band VII was designated as a novel phycocyanin-Chla/c2-protein complex （pI ≈ 3.4-3.7）. These results indicated that phycocyanin is structurally and functionally coupled with chlorophyll-protein complex in C. placoidea, and probably interacted with electrostatic force in combination.
基金Supported by the Natural Science Foundation of Shandong Province(No.ZR2018LD009)。
文摘An active photosystem(PS)Ⅱparticle and two light-harvesting complexes,as well as their subcomplexes that have not been reported previously,were isolated from a cryptophyte Chroomonas placoidea by Triton X-100 sucrose density gradient centrifugation.The fluorescence spectra revealed that there were efficient energy couplings between phycocyanin(PC645)and chlorophyll(Chl)within both zonesⅢandⅣof the gradient,which were designated respectively as light-harvesting complex and PSⅡparticles whose size was 15-20 nm according to negative staining in electron microscopy.When the two complexes were further resolved into sub-complexes,the energy coupling was retained in the core PSⅡcomplex(named as zoneⅣ-2 of the sucrose gradient),which contained almost no outer antenna pigment Chl c.Sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE)showed that the PC645 components appeared in Chl-containing protein complexes were mainly the β subunit with molecular weight of 20 kDa.These results demonstrate that PC645 in this cryptophyte was structurally but preferentially combined with the light-harvesting complex and PSⅡcore.The excitation energy absorbed by PC645 could be directly transferred to Chl a(especially the long wavelength of Chl a)in the PSⅡreaction center or via the Chl a/c-protein complex.The β subunit corresponded to the terminal fl uorescence emission and might play an important role in transmitting energy from PC645 to the Chl-protein complex.The results will help in elucidating the architecture and function of the energy transfer system comprising phycobiliproteins and Chl-protein complexes in cryptophytes.
基金granted by the National Science Fund of China(No.40976083)
文摘A new phycocyanin（PC） fluorescent subunit namedβ_2（18kDa） was isolated and characterized by both SDS-PAGE and isoelectric focusing（IEF） from a species of cryptophytic alga Chroomonas placoidea.PC was separated and purified by ammonium sulfate sedimentation followed by two steps of Sephadex G-100 chromatography.After denatured in 4 mol/L urea for 48 h,PC was divided into two fractions by passing through a Sephacryl S-100 chromatography column twice.The blue fraction（S-1） containedβsubunits with a maximal absorbance at 595 nm in visible light region.While the green fraction（S-2） enriched inαsubunits showed a characteristic long wavelength absorbance at 680-700 nm region and exhibited a relatively low molecular weight of 9.4（α_1） and 8.5 kDa（α_2）.Fraction S-1 also consisted of two different fluorescent subunits with molecular weight of 20.1 kDa（β_1） and 18 kDa （β_2） and differed from each other on isoelectric points of pH 5.7（ft） and 6.0（ft）,respectively.Further investigation of peptide sequence will help a lot in elucidating the new subunit ft that was smaller in size and more neutral than the known ft subunit,and may provide an alternative explanation in structure of cryptophytic phycobiliproteins.
