R-phycoerythrin was isolated and purified from a red alga, Polysiphonia 
urceolata Grev, using Streamline column combined with ion-exchange 
chromatography or hydroxyapatite chromatography. The purity of R-phycoerythrin 
isolated by Streamline column was up to 1.66 and the yield of R-phycoerythrin 
could be as high as 0.68 mg/g frozen P. urceolata. All the eluates from 
Streamline column were divided into two equivalent parts, respectively. One part 
was pumped into the ion-exchange column loaded with Q-Sepharose and the other 
was applied to the adsorption column loaded with hydroxyapatite. The purities of 
R-phycoerythrin purified using these two methods were both up to 3.26, more than 
3.2 the commonly accepted criterion. The yield of purified R-phycoerythrin from 
the ion-exchange chromatography was 0.40 mg/g frozen P. urceolata and that from 
the hydroxyapatite chromatography could reach 0.34 mg/g frozen P. urceolata. The 
purified protein had three absorption peaks at 498, 535, and 565 nm and 
displayed a fluorescence maximum at 580 nm, which was consistent with the 
typical spectrum of R-phycoerythrin. The purified R-PE was also identified with 
electrophoresis. Only one single protein band appeared on native-PAGE with 
silver staining. SDS-PAGE demonstrated the presence of one 20 kDa major subunit, 
and one low intensity band corresponding to 33 kDa subunit. The results indicate 
that using the expanded bed adsorption combined with ion-exchange chromatography 
or hydroxyapatite chromatography, R-phycoerythrin can be purified from frozen P. 
urceolata on large scale.