Amino acid sequence of the ß-subunit of phycoerythrin from the cryptophyte algae Chroomonas CS 24

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. © 1992.