As a step toward developing the tools needed to study the molecular bases of light regulation of gene expression in dinoflagellates, light-harvesting peridinin-chlorophyll a-protein (PCP) complexes from Glenodinium sp. were purified and used to generate anti-PCP antibodies. Affinity purified anti-PCP antibodies were isolated from the crude anti-PCP antiserum resulting in improved specificity of immune reactions. The affinity purified anti-PCP antibodies were shown to react strongly and specifically with all major isoforms of PCP complexes in Glenodinium sp. cells, and were used to assess qualitative changes in the levels of PCP gene products in cells grown under different light conditions. Western blot analysis revealed a two- to three-fold increase in detectable PCP apoprotein in low light compared to high light grown cells. In vitro translation reactions supplied with total RNA from high and low light grown Glenodinium sp. cultures also showed an approximate twofold increase in translatable PCP mRNAs in low light grown cells as determined by immunoprecipitation of the primary translation products with affinity purified anti-PCP antibodies. In addition, PCP apoproteins appear to be encoded as larger pre-proteins, since the major immunoprecipitated products from in vitro translation are 23 and 22 kilodaltons, while mature PCP apoproteins are 15.5 kilodaltons. The parallel increases in PCP apoprotein and translatable PCP mRNAs indicate that light regulation of PCP complexes occurs at the level of PCP mRNA abundance.