Pigment-protein complexes of Bryopsis corticulans were separated by PAGE and sucrose gradient centrifugation, and its characteristics were also investigated. Results showed that seven pigment-protein complexes were obtained by PAGE, which were CPIa1, CPIa2, CP I, LHCP1, LHCP2, CPa, LHCP3+3, and two free pigment bands(FP)Fca、FC. Five zones were separated by improved discontinuous sucrose gradient centrifugation. It indicated that zone Ⅰ was FP;zone Ⅱ was a light-harvesting complexes of PSⅡ with lower molecular weight as LHCP3+3, zone Ⅲ was aggregated light-harvesting complexes of PS Ⅱ as LHCP1. Both zone Ⅱ and Ⅲ contained large amount of Chlb and sinphonaxanthin except Chla, suggesting that they were characteristic of sinphonaxanthin-Chla/b-protein complexes;zone Ⅳ showed only one band in PAGE, and there was shoulder peak of Chlb in absorption spectra, containing 66 and 56 kDa peptides, so it was small PS I complexes of CP I a.
[4] Anderson J M.1983.Chlorophyll protein complexes of a Codium species including a light-harvesting siphonaxanthin-chlorophyll a/b protein complexes, an evolutionary relic of some Chlorophyta[J].Biochim Biophys Acta, 724:370-380.
[5] Arnon DI.1949.Copper enzymes in isolated chloroplasts pholyphenoloxidase in Beta vulgaris[J].Plant Physiol, 24:1-15.
