Isolation and characterization of R-phycoerythrin subunits and enzymatic digests.
Subunits and enzymatic digests of the highly fluorescent phycobiliprotein R-phycoerythrin (R-PE) were analyzed by several separation and detection techniques including HPLC, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), CE, and HPLC-electrospray ionization (ESI) MS. R-PE subunits were isolated by HPLC and detected as single molecules by total internal reflection fluorescence microscopy. The results show efficient absorption and fluorescence of the R-PE subunits and digest peptides, originating from the incorporation of phycoerythrobilin and phycourobilin chromophores in them. In addition, HPLC-ESI-MS and SDS-PAGE were optimized to determine the molecular masses of phycobiliprotein subunits and the chromophore-containing peptides, as well as the amino acid sequences of the latter. Favorable spectroscopic and structural properties of R-PE subunits and enzymatic digests, even under denaturing conditions, make these molecules suitable for use as fluorescence labels for biomolecules.[1]References
- Isolation and characterization of R-phycoerythrin subunits and enzymatic digests. Isailovic, D., Li, H.W., Yeung, E.S. Journal of chromatography. A. (2004) [Pubmed]
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