Ontogeny of the 35K epsilon crystallin during Rana temporaria lens development.
Epsilon is a recently described eye lens protein from Rana temporaria, an anuran amphibian. It is oligomeric with a subunit M.W. of 35K. The cDNA coding for 35K E- in frog lens does not show any homology with cDNA's coding for alpha-, beta-, gamma-, and delta-crystallins. Immunologically, it also does not react with antibodies directed against alpha-, beta-, and gamma-crystallins. The ontogeny of this 35K E-protein has been investigated in R. temporaria lens development by the indirect immunofluorescence staining method with an antibody specific for the 35K E-protein. The purity of the isolated 35K protein and the specificity of the antibody were controlled by Tris-SDS gel electrophoresis and immuno-blotting, respectively. The first positive immunofluorescence reaction was observed in the inner cell wall of a stage V lens. In the external layer/epithelium the reaction was first detected in a single cell of a stage VII lens. Additional positive cells in the external layer/epithelium were detected at an early state VIII and the reaction appeared to be patchy. This type of patchy reaction was also observed in the epithelium of froglet (sub-adult) eye lens.
D000818:Animals; D003459:Crystallins / Q000096:biosynthesis*; D004586:Electrophoresis; D005455:Fluorescent Antibody Technique; D007908:Lens, Crystalline / Q000254:growth & development* / Q000378:metabolism; D008970:Molecular Weight; D011896:Rana temporaria / Q000254:growth & development* / Q000378:metabolism
D003459:Crystallins