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An R-phycoerythrin (R-PE) was isolated by gel filtrations on Sepharose CL-4B and Sephadex G-150 from the phycobiliprotein extract of the marine red macroalga  Polysiphonia urceolata  Grev and further purified by ion exchange chromatography on DEAE-Sepharose Fast Flow. The purified R-PE showed three absorption peaks at 498 nm, 538 nm, 566 nm and one fluorescent emission maximum at 577 nm. Although the R-PE showed a single band on the examination by native PAGE, it exhibited two very close bands at pH about 4.7 in native isoelectric focusing (IEF). Polypeptide analysis of the R-PE demonstrated that it contained four chromophore-carrying subunits, α 18.2 , β 20.6 , γ 31.6  (γ'), γ 34.6  (γ), and no colorless polypeptide; its subunit composition was 6α 18.2 :6β 20.6 :1 γ 31.6 :2γ 34.6 . The α and β subunits were distributed within a acidic pH range from 5.0 to 6.0 in denaturing IEF and the γ subunits were in a basic pH range from 7.6 to 8.1. These results reveal that the prepared R-PE may exist in two hexamers of γ (αβ) 3  γ (αβ) 3 γ' and γ (αβ) 3  γ'(αβ) 3  γ and that the R-PE participate in the rod domain assembly of  P .  urceolata  phycobilisomes by stacking each of its trimer (αβ) 3  face-to-face with the aid of one γ subunit (γ or γ').

Characteristics of an R-Phycoerythrin with Two γ Subunits Prepared from Red Macroalga Polysiphonia urceolata