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

Autor: Jasminka Godovac-Zimmermann, Roger G. Hiller, Margaret Sheil, Pamela M. Wrench
Rok vydání: 1992
Předmět:
Zdroj: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1120:117-121
ISSN: 0167-4838
DOI: 10.1016/0167-4838(92)90432-d
Popis: The full amino acid sequence of the beta-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 phi beta-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 beta-subunits of the holoprotein are identical.
Databáze: OpenAIRE
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