Isolation and spectral characterization of phycobiliproteins.
Several phycobiliproteins were prepared chromatographically pure and their absorption, fluorescence-emission, fluorescence-excitation and fluorescence-excitation polarization spectra determined. Changes in these spectra with ionic strength of the aqueous medium and chromoprotein concentration were interpreted in terms of interchromophore energy transfer and protein subunit equilibria. The complexity of the polarization spectra confirms the presence of different types of chromophore, designated sensitizing (;s') and fluorescing (;f'), in a single protein.
D011232:Chemical Precipitation; D002848:Chromatography, DEAE-Cellulose; D056890:Eukaryota / Q000032:analysis*; D005453:Fluorescence; D010940:Plant Proteins / Q000302:isolation & purification*; D011758:Pyrroles; D013057:Spectrum Analysis
D010940:Plant Proteins; D011758:Pyrroles