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

Jasminka Godovac-Zimmermann*, Margaret Sheil, Pamela M. Wrench, Roger G. Hiller

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


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 languageEnglish
Pages (from-to)117-121
Number of pages5
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Issue number1
Publication statusPublished - 27 Mar 1992


  • (chroomonas CS24)
  • algae
  • amino acid sequence
  • chromophore
  • phycobiliprotein

Fingerprint Dive into the research topics of 'Amino acid sequence of the <i>β</i>-subunit of phycoerythrin from the cryptophyte algae Chroomonas CS 24'. Together they form a unique fingerprint.

Cite this