[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.
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D000368:Aged; D000369:Aged, 80 and over; D002352:Carrier Proteins; D002386:Cataract / Q000378:metabolism*; D003459:Crystallins / Q000032:analysis* / Q000302:isolation & purification; D015180:Electrophoresis, Gel, Two-Dimensional; D006801:Humans; D007908:Lens, Crystalline / Q000032:analysis*; D008970:Molecular Weight; D011952:Receptors, Concanavalin A / Q000032:analysis*
D002352:Carrier Proteins; D003459:Crystallins; D011952:Receptors, Concanavalin A; C027774:concanavalin A-binding glycoproteins