Abstract:Phycobilisome is the major accessory light-harvesting supramolecular complexes,which is composed of core and peripheral rods.Furthermore,the core contains several cylindrical protein assemblies that mainly consist of allophycocyanin,and is involved in the transfer of light energy to the reaction centers of photosystems.In this study,the apcA gene was amplified from the unicellular cyanobacterium Synechocystis sp.strain PCC 6803.The expression plasmid pET-32a(+)-apcA was constructed and transformed into BL21(DE3)pLysS,and the expression of ApcA protein was induced by IPTG.After purification by His-tag,the recombinant protein pET-ApcA was used to immunize Japanese White Rabbit to obtain the polyclonal antibody.The titer of the polyclonal antibody was detected by ELISA and its specificity was analyzed by immunoblotting.The titer of polyclonal antibody was found to be up to 1∶1 025 000,and thus possessed a high specificity.A polyclonal allophycocyanin antibody of Synechocystis 6803 was successfully obtained in this study,and it will further help in understanding the important roles of core of cyanobacterial phycobilisome during light energy transfer by using biochemical strategy.