Quantification of chromophore pigments, apoprotein abundance and isoelectric variants of peridinin-chlorophyll a-protein complexes (PCPs) in the dinoflagellate Heterocapsa pygmaea grown under variable light conditions
1992
Jovine, R.V.M. | Triplett, E.L. | Nelson, N.B. | Prezelin, B.B.
Absorption properties, pigmentation, total protein, apoprotein content, and isoelectric diversity of Peridinin-Chlorophyll a-Protein complexes (PCPs) and their apoproteins were determined for Heterocapsa pygmaea populations photoadapted to different spectral irradiances. Chromatic adaptation of pigmentation was evident and correlated more with quanta absorbed by the cells (AQ cell(-1)) than with quanta available in the surrounding light field (Qpar). Peridinin and chlorophyll content increased as blue-green and red light dosages declined respectively. Immunological determinations indicated PCP apoprotein abundance increased as AQ cell(-1) decreased, while non-PCP protein content was unchanged. PCP apoproteins could account for up to 30% of total protein and exceed by 10-fold the amount required to bind all peridinin molecules into PCP complexes. Isoelectric variants of PCPs were identified, whose relative abundances were light dependent. Results are discussed in the context of future photoregulation studies of PCP gene expression in dinoflagellates.
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