Ontogeny of the 38K ϵ-polypeptide during lens development of the duckAnas platyrhynchos

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Abstract
The .epsilon.-crystallin polypeptide is a recently described protein in the eye lens of the peking duck, A. platyrhynchos (1). It does not cross react with .alpha.-, .beta.-, .delta.-, and .gamma.-crystallins. It has a MW of 120K and consists of 3 identical 38K polypeptides. It is found in some reptiles and birds. The ontogeny of this polypeptide was investigated in the developing A. platyrhynchos lens via the indirect immunofluorescence staining using a homologous antibody. The 38K polypeptide was extracted from 13% Tris-SDS [sodium dodecyl sulfate] acrylamide gels, lyophilized and injected into a young rabbit to raise an antibody. The purity of the isolated 38K polypeptide and and the specificity of the antibody were checked by Tris-SDS gel electrophoresis and immunoblotting, respectively. The 1st positive reaction was detected at 80 h (stage 18) incubated lens. It was confined to a few elongating early primary fibers. Until the 9th day of development the reaction is confined to the primary and secondary lens fibers. The first positive reaction in the annular pad area is observed in day 10 lens. In the anterior epithelium the 1st positive reaction was detectable in day 12 lens. At the beginning it was confined to a few cells in the center of the epithelium and gradually the reaction spreads to other cells. A strong and uniform reaction in the entire epithelium is noted for the 1st time in the lens of a just-hatched duckling. The 38K .epsilon.-polypeptide is detectable after the .alpha.-, .beta.-, and .delta.-crystallins, which, in the duck, appear simultaneously from 66 h (stage 15/16).