A covalent change in alpha crystallin during opacification of the Emory mouse lens.

Polyclonal antisera made against synthetic peptides corresponding to the N-terminus (anti-alpha NT), the C-terminus (anti-alpha CT), and to an internal sequence (anti-alpha 147-161) of bovine alpha-A2 crystallin have been used to quantitatively probe Western blots of proteins from the Emory mouse cataractous lens. Relative to proteins from transparent lenses of the control Carworth Farm Webster (CFW) mouse, there is no significant difference in binding of the anti-alpha NT and anti-alpha CT sera to alpha crystallin from lenses of cataractous Emory mice versus transparent lenses of CFW mice at any of the ages studied. In contrast, antiserum to an internal sequence (anti-alpha 147-161) binds significantly better to alpha crystallin from cataractous Emory mice lenses. Together, these results demonstrate covalent changes in the alpha crystallin molecule during opacification of the Emory mouse lens, which like those occurring in the human senile cataractous lens, result in increased binding of the anti-alpha 147-161 serum.