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Abstract
Polyclonal antiserum has been made against beta crystallin from human lens, and against synthetic peptides corresponding to the N- and C-terminal sequences of bovine beta Bp crystallin. A solid-phase radioimmunoassay has been used to quantitate binding of these antisera to soluble proteins from microdissected sections. The results of this analysis demonstrate the feasibility of using radioimmunoassay analysis in combination with peptide antisera to determine statistically significant changes in protein antigenicity from opaque versus transparent regions from the same human cataractous lens.