Abstract
The ontogeny of .alpha.A, .alpha.B and .alpha.Ains polypeptides of the .alpha.-crystallin was investigated by the indirect immunofluorescence staining method with antibodies directed against these three polypeptides in a mutant mouse strain called dyl. In this strain cataractogenesis starts around day 16 of lens development but the early development of the lens and the ontogeny of lens crystallins do not differ from the normal genotype. The polypeptides were fractionated from normal adult Swiss albino mice total native .alpha.-crystallin by SDS gel electrophoresis, extracted, lyophilized and injected into young rabbits for production of the antibody. The isolated polypeptides were controlled by SDS gel re-electrophoresis and the antibodies were tested against rat lens native .alpha.-crystallin by immunoblotting. .alpha.A and .alpha.Ains antibodies cross reacted, while .alpha.B did not show any cross reaction. Results presented here show that .alpha.A and .alpha.B appear simultaneously while .alpha.Ains was detectable at a later stage of lens development. These results are discussed.