Science in China Series C: Life Sciences

, Volume 41, Issue 1, pp 9–17 | Cite as

Isolation, properties and spatial site analysis of γ subunits of B-phycoerythrin and R-phycoerythrin

  • Guangce Wang
  • Baicheng Zhou
  • Chengkui Zeng


Polysiphonia urceolata R-phycoerythrin andPorphyridium cruentum B-phycoerythrin were degraded with proteinaseK, and then the nearly native γ subunits were isolated from the reaction mixture. The process of degradation of phycocrythrin with proteinaseK showed that the γ subunit is located in the central cavity of (αβ)6 hexamer of phycoerythrin. Comparative analysis of the spectra of the native phycoerythrin, the phycoerythrin at pH 12 and the isolated γ subunit showed that the absorption peaks of phycoerythrobilins on α or β subunit are at 535 nm (or 545 nm) and 565 nm, the fluorescence emission maximum at 580 nm; the absorption peak of phycoerythrobilins on the isolated γ subunit is at 589 nm, the fluorescence emission peak at 620 nm which overlaps the absorption maximum of C-phycocyanin and perhaps contributes to the energy transfer with high efficiency between phycoerythrin and phycocyanin in phycobilisome; the absorption maximum of phycourobilin on the isolated γ subunit is at 498 nm, which is the same as that in native phycoerythrin, and the fluorescence emission maximum at 575 nm.


B-phycoerythrin R-phycoerythrin γ subunit spectroscopic properties 


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Copyright information

© Science in China Press 1998

Authors and Affiliations

  • Guangce Wang
    • 1
  • Baicheng Zhou
    • 1
  • Chengkui Zeng
    • 1
  1. 1.Experimental Marine Biology Laboratory, Institute of OceanologyChinese Academy of SciencesQingdaoChina

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