Abstract
The full amino acid sequence of the ß-subunit of Chroomonas CS24 phycoerythrin has been determined by conventional Edman degradation and mass spectrometry. The sequence compromises 177 amino acids with a molecular mass of 18669 Da. It is 91.5% identical to the deduced amino acid sequence of Cryptomonas Φ ß-phycoerythrin (Reith, M. and Douglas, S. (1990) Plant Mol. Biology 15, 585-592). The chromophores are bound by single thioether linkages. No evidence of microheterogeneity was found confirming that both ß-subunits of the holoprotein are identical.
Original language | English |
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Pages (from-to) | 117-121 |
Number of pages | 5 |
Journal | Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular |
Volume | 1120 |
Issue number | 1 |
DOIs | |
Publication status | Published - 27 Mar 1992 |
Keywords
- (chroomonas CS24)
- algae
- amino acid sequence
- chromophore
- phycobiliprotein