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Peridinin-chlorophyll a proteins of the dinoflagellate Amphidinium carterae (Plymouth 450)

Journal Article · · Plant Physiol.; (United States)
DOI:https://doi.org/10.1104/pp.57.2.297· OSTI ID:7145071
The marine dinoflagellate Amphidinium carterae (Plymouth 450) releases several water-soluble peridinin-chlorophyll a proteins after freeze-thawing. These chromoproteins have a molecular weight of 39.2 x 10/sup 3/ 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 percent of the extractable peridinin-chlorophyll a protein. It consists of an alanine-rich apoprotein of molecular weight 31.8 x 10/sup 3/ 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.
Research Organization:
Brookhaven National Lab., Upton, NY
OSTI ID:
7145071
Journal Information:
Plant Physiol.; (United States), Journal Name: Plant Physiol.; (United States) Vol. 57:2; ISSN PLPHA
Country of Publication:
United States
Language:
English