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

doi:10.1016/0167-4838(92)90432-D

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 journal › Article › peer-review

3 Citations (Scopus)

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.

Original language	English
Pages (from-to)	117-121
Number of pages	5
Journal	Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume	1120
Issue number	1
DOIs	https://doi.org/10.1016/0167-4838(92)90432-D
Publication status	Published - 27 Mar 1992

Keywords

(chroomonas CS24)
algae
amino acid sequence
chromophore
phycobiliprotein

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10.1016/0167-4838(92)90432-D

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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.",

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T1 - Amino acid sequence of the β-subunit of phycoerythrin from the cryptophyte algae Chroomonas CS 24

AU - Godovac-Zimmermann, Jasminka

AU - Sheil, Margaret

AU - Wrench, Pamela M.

AU - Hiller, Roger G.

PY - 1992/3/27

Y1 - 1992/3/27

N2 - 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.

AB - 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.

KW - (chroomonas CS24)

KW - algae

KW - amino acid sequence

KW - chromophore

KW - phycobiliprotein

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JO - Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

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

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Keywords

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