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 |
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Rok vydání: | 1992 |
Předmět: |
chemistry.chemical_classification
Molecular mass Edman degradation biology Phycobiliprotein Molecular Sequence Data Biophysics Eukaryota Phycoerythrin Chroomonas biology.organism_classification Biochemistry Amino acid Molecular Weight Cryptomonas chemistry Structural Biology biology.protein Chymotrypsin Trypsin Amino Acid Sequence Molecular Biology Peptide sequence |
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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