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

Journal Article


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. © 1992.

UOW Authors


  •   Sheil, Margaret (external author)

Publication Date


  • 1992

Citation


  • Godovac-Zimmermann, J., Sheil, M., Wrench, P. M., & Hiller, R. G. (1992). Amino acid sequence of the ß-subunit of phycoerythrin from the cryptophyte algae Chroomonas CS 24. Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, 1120(1), 117-121. doi:10.1016/0167-4838(92)90432-D

Scopus Eid


  • 2-s2.0-0026597694

Start Page


  • 117

End Page


  • 121

Volume


  • 1120

Issue


  • 1

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. © 1992.

UOW Authors


  •   Sheil, Margaret (external author)

Publication Date


  • 1992

Citation


  • Godovac-Zimmermann, J., Sheil, M., Wrench, P. M., & Hiller, R. G. (1992). Amino acid sequence of the ß-subunit of phycoerythrin from the cryptophyte algae Chroomonas CS 24. Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, 1120(1), 117-121. doi:10.1016/0167-4838(92)90432-D

Scopus Eid


  • 2-s2.0-0026597694

Start Page


  • 117

End Page


  • 121

Volume


  • 1120

Issue


  • 1