Photostability studies of phycobiliprotein fluorescent labels.
Photostability studies of four fluorescent phycobiliproteins were conducted to identify stable chromophores for biological labeling applications. Phycobiliprotein photodestruction was linear with the applied laser power and depended on the total number of photons absorbed per molecule. Photodestruction quantum yields phi of 1.1 X 10(-5) for R-phycoerythrin, 6.6 X 10(-6) for B-phycoerythrin, 4.5 X 10(-6) for allophycocyanin, and 2.5 X 10(-6) for C-phycocyanin were measured. C-Phycocyanin is a factor of 10.8 more photostable than fluorescein. The photostability of R-phycoerythrin was improved by a factor of 1.7 by adding n-propyl gallate. The addition of superoxide dismutase, catalase, sodium dithionite, ascorbate, dithiothreitol, EDTA, or deoxygenation with argon bubbling had no effect on the photostability of R-phycoerythrin.
D002374:Catalase / Q000494:pharmacology; D005456:Fluorescent Dyes; D045342:Light-Harvesting Protein Complexes; D010777:Photochemistry; D010798:Phycocyanin / Q000494:pharmacology; D010799:Phycoerythrin / Q000494:pharmacology; D010940:Plant Proteins; D011435:Propyl Gallate / Q000494:pharmacology; D013482:Superoxide Dismutase / Q000494:pharmacology
D005456:Fluorescent Dyes; D045342:Light-Harvesting Protein Complexes; D010940:Plant Proteins; D010798:Phycocyanin; D010799:Phycoerythrin; D011435:Propyl Gallate; D002374:Catalase; D013482:Superoxide Dismutase