High molecular weight aggregates from human cataracts: characterization by Western blot analysis.
The formation of covalently linked, high molecular weight protein aggregates has been thought to play an important role in opacification of the human lens. Antisera were used in Western blot analysis to demonstrate the involvement of all major classes of lens proteins (alpha, beta and gamma crystallin; the major intrinsic membrane polypeptide) in covalent aggregation. Of these classes, aggregation of gamma and beta crystallins via intermolecular disulfide bonding and aggregation of the major intrinsic membrane polypeptide via intermolecular, non-disulfide bonding were more pronounced in cataractous as compared with normal lenses.
D002386:Cataract / Q000378:metabolism*; D003459:Crystallins / Q000302:isolation & purification*; D004220:Disulfides / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007106:Immune Sera; D046911:Macromolecular Substances; D008970:Molecular Weight; D012016:Reference Values
D003459:Crystallins; D004220:Disulfides; D007106:Immune Sera; D046911:Macromolecular Substances