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

Department of Biological Sciences

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

Access to Document

10.1016/0167-4838(92)90432-D

Link to publication in Scopus

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

@article{af1b59224ca843a9b0c9ea59dc199ac9,

title = "Amino acid sequence of the β-subunit of phycoerythrin from the cryptophyte algae Chroomonas CS 24",

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.",

keywords = "(chroomonas CS24), algae, amino acid sequence, chromophore, phycobiliprotein",

author = "Jasminka Godovac-Zimmermann and Margaret Sheil and Wrench, {Pamela M.} and Hiller, {Roger G.}",

year = "1992",

month = mar,

day = "27",

doi = "10.1016/0167-4838(92)90432-D",

language = "English",

volume = "1120",

pages = "117--121",

journal = "Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology",

issn = "0167-4838",

publisher = "Elsevier",

number = "1",

}

TY - JOUR

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

UR - http://www.scopus.com/inward/record.url?scp=0026597694&partnerID=8YFLogxK

U2 - 10.1016/0167-4838(92)90432-D

DO - 10.1016/0167-4838(92)90432-D

M3 - Article

C2 - 1554738

AN - SCOPUS:0026597694

VL - 1120

SP - 117

EP - 121

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

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

SN - 0167-4838

IS - 1

ER -