[Heterogeneity of human cataractous lens low molecular weight crystallins--study of concanavalin A binding proteins by two-dimensional electrophoresis].

Low molecular weight proteins (beta s, gamma H and gamma L crystallins) were fractionated from human cataractous lens using gel filtration of Sephadex G-75 column chromatography. Each crystallin was separated by two-dimensional electrophoresis and identified by Coommassie blue staining and Concanavalin A binding. Several components of beta s, gamma H and gamma L-crystallins stained with Coomassie blue did not bind with Concanavalin A. Two-dimensional electrophoresis revealed heterogeneities of all three low molecular weight crystallins. This phenomenon may be due to differences in the amount of bound glucose and mannose.