Ontogeny of the 35K epsilon crystallin during Rana temporaria lens development
作者:
BrahmaS. K.,
McDevittD. S.,
DefizeL. H.K.,
期刊:
Current Eye Research
(Taylor Available online 1986)
卷期:
Volume 5,
issue 10
页码: 739-743
ISSN:0271-3683
年代: 1986
DOI:10.3109/02713688609000014
出版商: Taylor&Francis
数据来源: Taylor
摘要:
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 35Kϵ- in frog lens does not show any homology with cDNA's coding forα,β,γandδ-crystallins. Immunologically, it also does not react with antibodies directed againstα,β-, andγ-crystallins (1).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 (2) and immuno-blotting, respectively (3).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 VI1 lens. Additional positive cells in the external layer/epithelium were detected at an early stage Vlll and the reaction appeared to be patchy. This type of patchy reaction was also observed in the epithelium of froglet (sub-adult) eye lens.
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