Cation-induced aggrcgation of isolated LHC2 was ušed to compare the adliesion- promoting activities of individual LHCP2. Precipitated and waslied LHC2 of camation origin was aggregated in the presence of KCl. The polypeptide composition of the LHC2 sheets remaining in non-aggregated form after different tiine intervals was analysed by SDS-PAGE followed by scanning laser densitometiy. The LHC2 sheets enriched in a major camation LHC2-27 kDa polypeptide were shown to aggregate at a faster rate than the sheets enriched in minor LHCP2, i.e. 26 and 23 kDa polypeptides, although the finál degree of aggrcgation was similar for all types of LHC2 sheets.