Covalent changes at the N- and C-terminal regions of gamma crystallin during aging of the normal human lens.

Polyclonal antisera have been made to synthetic peptides corresponding to the N- and C-terminal regions of the putative gamma 1-2 gene from human lens. These antisera are specific for gamma crystallin, showing no cross-reactivity with any polypeptides of the alpha- and beta-crystallin fractions. Western blot analysis demonstrates a dramatic decrease in the binding of these antisera to gamma crystallin during aging of the normal human lens, while identical analysis with polyclonal antisera to the major cyanogen bromide fragment (19,000 MW) of human gamma crystallin shows little, if any, change during aging. Together, these demonstrate that antisera to synthetic peptides of the N- and C-terminal regions of the gamma 1-2 gene are very specific probes that can demonstrate extensive covalent modification from both ends of the gamma crystallin molecule during aging of the normal human lens.