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Plant and Cell Physiology, 1982, Vol. 23, No. 5 785-790
© 1982

Article

Chlorophyll-Protein Complexes in Salix sp. ‘Aquatica Gigantea’ under Strong and Weak Light I. Spectral Characterization of the Chlorophyll-Protein Complexes

Arja Nurmi1 and Elina Vapaavuori2

1Department of Botany, University of Helsinki Unioninkatu 44, SF-00170 Helsinki 17, Finland
2The Finnish Forest Research Institute, Suonenjoki Research Station SF-77600 Suonenjoki, Finland

The distribution of chlorophyll in the chlorophyll-protein complexes was studied in Salix sp. ‘aquatica gigantea’ grown under high and low irradiance. The chlorophyll- containing bands that could be separated by SDS-polyacrylamide gel electrophoresis in strong and weak light numbered 9 to 13 and 9 to 11, respectively. In strong light the following bands were separated, in the order of the highest to the lowest molecular weight: one to two chlorophyll a/b-protein complexes, three to four chlorophyll a-containing bands similar to the P700-chlorophyll a-protein complex (CPI and its oligomers), three oligomers of the light-harvesting chlorophyll a/b-protein complex (LHCP***, LHCP**, LHCP*), two chlorophyll a-protein complexes (CPa2 and CPa1), the light-harvesting chlorophyll a/b-protein complex (LHCP) and the protein free pigment (FP). In weak light the same chlorophyll-containing bands were separated with the exception that no high molecular weight chlorophyll a/b-protein complexes could be observed. In strong light the CPI complexes were the largest structural component of the chloroplast lamellae. In weak light the LHCP complexes together contributed the major proportion of the total chlorophyll. The increase in the chlorophyll associated with the LHCP complex was possibly caused by reorganization of the lamellar structure or by increased synthesis of the LHCP** complex, which appeared to be a labile complex in weak light.

(Received February 1, 1982; Accepted May 10, 1982)
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