Subunit structure of the phycobiliproteins of blue-green algae.
The phycobiliproteins of the blue-green algae Synechococcus sp. and Aphanocapsu sp. were characterized with respect to homogeneity, isoelectric point, and subunit composition. Each of the biliproteins consisted of two different noncovalently associated subunits, with molecular weights of about 20,000 and 16,000 for phycocyanin, 17,500 and 15,500 for allophycocyanin, and 22,000 and 20,000 for phycoerythrin. Covalently bound chromophore was associated with each subunit.
D000818:Animals; D001654:Bile Pigments / Q000302:isolation & purification*; D011232:Chemical Precipitation; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003116:Color; D000458:Cyanobacteria / Q000032:analysis*; D004586:Electrophoresis; D005453:Fluorescence; D007106:Immune Sera; D005779:Immunodiffusion; D007525:Isoelectric Focusing; D046911:Macromolecular Substances; D008970:Molecular Weight; D010788:Photosynthesis; D010940:Plant Proteins / Q000302:isolation & purification*; D011485:Protein Binding; D000644:Quaternary Ammonium Compounds; D011817:Rabbits; D013431:Sulfates
D001654:Bile Pigments; D007106:Immune Sera; D046911:Macromolecular Substances; D010940:Plant Proteins; D000644:Quaternary Ammonium Compounds; D013431:Sulfates