Abstract
The mouse monoclonal antibodies, prepared with rat βH-crystall in as parent antigen, show cross-reactivity to specific subunits in βH-, βpLI-, and βL2-crystall in but no reactivity to either α-or γ-crystall ins. Antigenic homology among the β-crystall in subunits was demonstrated by comparison of the topographic distributions of peptides on two-dimensional electrophoretograms subjected to either staining or an ELISA of the inmunoblots.