Phycobilisome structure of porphyridium cruentum: polypeptide composition
Purified phycobilisomes of porphyridium cruentum were solubilized in sodium dodecyl sulfate and resolved by sodium dodecyl sulfate-acrylamide gel electrophoresis into nine colored and nine colorless polypeptides. The colored polypeptides accounted for about 84% of the total stainable protein, and the colorless polypeptides accounted for the remaining 16%. Five of the colored polypeptides ranging in molecular weight from 13,300 to 19,500 were identified as the ..cap alpha.. and ..beta.. subunits of allophycocyanin, R-phycocyanin, and phycoerythrin. Three others (29,000-30,500) were orange and are probably related to the ..gamma.. subunit of phycoerythrin. Sequential dissociation of phycobilisomes, and analysis of the polypeptides in each fraction, revealed the association of a 32,500 molecular weight colorless polypeptide with a phycoerythrin fraction. The remaining eight colorless polypeptides were in the core fraction of the phycobilisome, which also was enriched in allophycocyanin.
- Research Organization:
- Smithsonian Institution, Rockville, MD
- DOE Contract Number:
- AS05-76ER04310
- OSTI ID:
- 7192447
- Journal Information:
- Plant Physiol.; (United States), Journal Name: Plant Physiol.; (United States) Vol. 68; ISSN PLPHA
- Country of Publication:
- United States
- Language:
- English
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