Apoprotein Composition and Spectroscopic Characterization of the Water-Soluble Peridinin--Chlorophyll a--Proteins from Three Symbiotic Dinoflagellates
The water-soluble peridinin—chlorophyll a— proteins (sPCP) from three symbiotic dinoflagellates, Symbiodinium microadriaticum, S. kawagutii and S. pilosum, have been analysed for their quaternary structure (by using immunoblotting techniques) and spectroscopic characteristics (by using absorption an...
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Published in | Proceedings of the Royal Society. B, Biological sciences Vol. 246; no. 1317; pp. 275 - 283 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
London
The Royal Society
23.12.1991
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Online Access | Get full text |
ISSN | 0962-8452 1471-2954 |
DOI | 10.1098/rspb.1991.0155 |
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Abstract | The water-soluble peridinin—chlorophyll a— proteins (sPCP) from three symbiotic dinoflagellates, Symbiodinium microadriaticum, S. kawagutii and S. pilosum, have been analysed for their quaternary structure (by using immunoblotting techniques) and spectroscopic characteristics (by using absorption and fluorescence spectra). The sPCP from S. kawagutii is comprised exclusively of a monomeric apoprotein of 35 kDa, whereas sPCP from S. pilosum possesses only a dimeric apoprotein with subunits of 15 kDa each. The sPCP from S.microadriaticum simultaneously contains both. Spectroscopically, sPCP from S. kawagutii is very similar to the 35 kDa species in S. microadriaticum', sPCP from S. pilosum is similar to the 15 kDa species from S. microadriaticum. Gaussian deconvolution analyses of absorption and fluorescence emission spectra show that each holoprotein is comprised of two spectrally distinct forms of chlorophyll a. We propose m olecular topologies for sPCP consistent with our findings. |
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AbstractList | The water-soluble peridinin--chlorophyll a--proteins (sPCP) from three symbiotic dinoflagellates, Symbiodinium microadriaticum, S. kawagutii and S. pilosum, have been analysed for their quaternary structure (by using immunoblotting techniques) and spectroscopic characteristics (by using absorption and fluorescence spectra). The sPCP from S. kawagutii is comprised exclusively of a monomeric apoprotein of 35 kDa, whereas sPCP from S. pilosum possesses only a dimeric apoprotein with subunits of 15 kDa each. The sPCP from S. microadriaticum simultaneously contains both. Spectroscopically, sPCP from S. kawagutii is very similar to the 35 kDa species in S. microadriaticum; sPCP from S. pilosum is similar to the 15 kDa species from S. microadriaticum. Gaussian deconvolution analyses of absorption and fluorescence emission spectra show that each holoprotein is comprised of two spectrally distinct forms of chlorophyll a. We propose molecular topologies for sPCP consistent with our findings. The water-soluble peridinin—chlorophyll a— proteins (sPCP) from three symbiotic dinoflagellates, Symbiodinium microadriaticum, S. kawagutii and S. pilosum, have been analysed for their quaternary structure (by using immunoblotting techniques) and spectroscopic characteristics (by using absorption and fluorescence spectra). The sPCP from S. kawagutii is comprised exclusively of a monomeric apoprotein of 35 kDa, whereas sPCP from S. pilosum possesses only a dimeric apoprotein with subunits of 15 kDa each. The sPCP from S.microadriaticum simultaneously contains both. Spectroscopically, sPCP from S. kawagutii is very similar to the 35 kDa species in S. microadriaticum', sPCP from S. pilosum is similar to the 15 kDa species from S. microadriaticum. Gaussian deconvolution analyses of absorption and fluorescence emission spectra show that each holoprotein is comprised of two spectrally distinct forms of chlorophyll a. We propose m olecular topologies for sPCP consistent with our findings. The water-soluble peridinin--chlorophyll a--proteins (sPCP) from three symbiotic dinoflagellates, Symbiodinium microadriaticum, S. kawagutii and S. pilosum, have been analysed for their quaternary structure (by using immunoblotting techniques) and spectroscopic characteristics (by using absorption and fluorescence spectra). The sPCP from S. kawagutii is comprised exclusively of a monomeric apoprotein of 35 kDa, whereas sPCP from S. pilosum possesses only a dimeric apoprotein with subunits of 15 kDa each. The sPCP from S. microadriaticum simultaneously contains both. Spectroscopically, sPCP from S. kawagutii is very similar to the 35 kDa species in S. microadriaticum; sPCP from S. pilosum is similar to the 15 kDa species from S. microadriaticum. Gaussian deconvolution analyses of absorption and fluorescence emission spectra show that each holoprotein is comprised of two spectrally distinct forms of chlorophyll a. We propose molecular topologies for sPCP consistent with our findings. |
Author | Govind, N. S. Trench, R. K. Iglesias-Prieto, R. |
Author_xml | – sequence: 1 givenname: R. surname: Iglesias-Prieto fullname: Iglesias-Prieto, R. organization: Department of Biological Sciences and The Marine Science Institute, University of California at Santa Barbara, Santa Barbara, California 93106, U. S. A – sequence: 2 givenname: N. S. surname: Govind fullname: Govind, N. S. organization: Department of Biological Sciences and The Marine Science Institute, University of California at Santa Barbara, Santa Barbara, California 93106, U. S. A – sequence: 3 givenname: R. K. surname: Trench fullname: Trench, R. K. organization: Department of Biological Sciences and The Marine Science Institute, University of California at Santa Barbara, Santa Barbara, California 93106, U. S. A |
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Snippet | The water-soluble peridinin--chlorophyll a--proteins (sPCP) from three symbiotic dinoflagellates, Symbiodinium microadriaticum,
S. kawagutii and S. pilosum,... The water-soluble peridinin—chlorophyll a— proteins (sPCP) from three symbiotic dinoflagellates, Symbiodinium microadriaticum, S. kawagutii and S. pilosum,... The water-soluble peridinin--chlorophyll a--proteins (sPCP) from three symbiotic dinoflagellates, Symbiodinium microadriaticum, S. kawagutii and S. pilosum,... |
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StartPage | 275 |
SubjectTerms | Absorption spectra Apoproteins Chlorophylls Emission spectra Fluorescence Molecules Room temperature Spectroscopic analysis Spectroscopy Symbiosis |
Title | Apoprotein Composition and Spectroscopic Characterization of the Water-Soluble Peridinin--Chlorophyll a--Proteins from Three Symbiotic Dinoflagellates |
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