CP26, CP29 and three different LHC II subcomplexes have been purified from a carnation photosystem II (PSII) preparation using non-denaturing isoelectric focusing in a vertical polyacrylamide slab gel. The identity of the fractions was established by absorption spectroscopy, SDS-PAGE and immunoblotting. CP26 comprised a single apoprotein of 26.6 kDa and CP29 contained two apoproteins of 28.8 and 28.5 kDa. LHC II subcomplex A consisted of Lhcb1 homotrimers, and subcomplexes B and C consisted of Lhcb1/Lhcb2 and Lhcb1/Lhcb3 heterotrimers, respectively. We discuss the data in relation to the organization of the PS II antenna in vivo.