Resolution of Chlorophyll a/b-Protein Complexes by Polyacrylamide Gel Electrophoresis: Evidence for the Heterogeneity of Light-Harvesting Chlorophyll a/b-Protein Complexes

Laboratory for Plant Ecological Studies, Faculty of Science, Kyoto University, Kyoto 606, Japan P700-Chl a-protein complexes (CP1 and CP1*), Chl-protein complexes of PS II core (CPa-1 and CPa-2), light-harvesting Chi a/A-protein complexes (LHCPo and LHCPm) and CP29 of spinach thylakoids were resolved by SDS-polyacrylamide-gel electrophoresis (PAGE) under non-denaturing conditions. The LHCP oligomer purified by electrophoresis, had 29.5- and 27-kDa polypeptides. CP1, CP29 and two LHCPs (LHCP-1 and LHCP-2) of spinach thylakoids were separated by a lithium dodecylsulfate (LDS) PAGE system with high resolution. The two LHCPs showed the same absorption spectrum on the gel. When LHCP oligomer was reelectrophoresed by this system it also gave LHCP-1, and LHCP-2. LHCP-1 had both 29.5- and 27- kDa polypeptides, but LHCP-2 had only 29.5 kDa polypeptide. Both polypeptides seemed to bind Chi. The heterogeneity of LHCP was also observed with bean thylakoids.