Plant Physiol. Illumina
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Plant Physiology 57:297-303 (1976)
© 1976 American Society of Plant Biologists

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (66)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Haxo, F. T.
Right arrow Articles by Siegelman, H. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Haxo, F. T.
Right arrow Articles by Siegelman, H. W.
Agricola
Right arrow Articles by Haxo, F. T.
Right arrow Articles by Siegelman, H. W.
Articles

Peridinin-Chlorophyll a Proteins of the Dinoflagellate Amphidinium carterae (Plymouth 450) 1

Francis T. Haxo2, J. Helen Kycia, G. Fred Somers3, Allen Bennett4 and Harold W. Siegelman

a Department of Biology, Brookhaven National Laboratory, Upton, New York 11973

The marine dinoflagellate Amphidinium carterae (Plymouth 450) releases several water-soluble peridinin-chlorophyll a proteins after freezethawing. These chromoproteins have a molecular weight of 39.2 x 103 and are comprised of noncovalently bound peridinin and chlorophyll a and a nonoligomeric protein. They have distinct isoelectric points and may be resolved into six components by either isoelectric focusing on polyacrylamide gel or ion exchange chromatography. The predominant chromoprotein, which has a pI of 7.5, constitutes about 90% of the extractable peridinin-chlorophyll a protein. It consists of an alanine-rich apoprotein of molecular weight 31.8 x 103 stoichiometrically associated with 9 peridinin and 2 chlorophyll a molecules. Additionally, the peridinin-chlorophyll a proteins with pI values of 7.6 and 6.4 were purified and found to have amino acid and chromophore composition essentially identical with the pI 7.5 protein. Peridinin-chlorophyll a protein, pI 7.5, after treatment at alkaline pH was transformed into several more acid pI forms of the protein, strongly suggesting that the naturally occurring proteins are deamidation products of a single protein. Fluorescence excitation and emission spectra demonstrate that light energy absorbed by peridinin induces chlorophyll a fluorescence presumably by intramolecular energy transfer. The peridinin-chlorophyll a proteins presumably function in vivo as photosynthetic light-harvesting pigments.

2 Permanent address: Scripps Institution of Oceanography, University of California, San Diego, Calif. 92093.

3 Permanent address: University of Delaware, Newark, Del. 19711.

4 Present address: University of Miami School of Medicine, Biscayne Annex, Miami, Fla. 33152.

1 Research was carried out at Brookhaven National Laboratory under the auspices of the United States Energy Research and Development Administration. A. Bennett was supported by a postdoctoral fellowship from the National Institutes of Health.




This article has been cited by other articles:


Home page
 Mol Biol EvolHome page
J. R. Reichman, T. P. Wilcox, and P. D. Vize
PCP Gene Family in Symbiodinium from Hippopus hippopus: Low Levels of Concerted Evolution, Isoform Diversity, and Spectral Tuning of Chromophores
Mol. Biol. Evol., December 1, 2003; 20(12): 2143 - 2154.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1976 by the American Society of Plant Biologists