Phycobilisome-associated glycoproteins in the cyanobacterium Anacystis nidulans R 2.
Four phycobilisome-associated proteins were found to be specifically reactive with the lectin concanavalin A after subunits of isolated Anacystis nidulans R 2 phycobilisomes were separated on polyacrylamide gels and transferred onto nitrocellulose. The concanavalin A-reactive phycobilisome components have proposed functions related to the orientation, assembly, and membrane attachment of the phycobilisome. Chemical analysis of the total isolated phycobilisome material indicated the presence of glucose (approx. 1.5% by wt) and N-acetylgalactosamine (0.15% by wt), consistent with our proposal that the concanavalin A-reactive polypeptides contain covalently linked, glucose-containing polysaccharides.
D000116:Acetylgalactosamine / Q000032:analysis; D000458:Cyanobacteria / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005947:Glucose / Q000032:analysis; D006023:Glycoproteins / Q000032:analysis / Q000378:metabolism*; D045342:Light-Harvesting Protein Complexes; D045524:Phycobilisomes; D010940:Plant Proteins / Q000032:analysis / Q000378:metabolism*; D013194:Staining and Labeling
D006023:Glycoproteins; D045342:Light-Harvesting Protein Complexes; D045524:Phycobilisomes; D010940:Plant Proteins; D005947:Glucose; D000116:Acetylgalactosamine