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Abstract
Zone electrophoresis in agar gel and immunoelectrophoresis were used to study the soluble lens proteins (crystallins) during embryonic and postnatal development of different vertebrates. With these methods, the first soluble lens proteins were detectable when the cells of the retinal side of the lens vesicle began to elongate, and the primary lens fibers were differentiating. There were considerable differences in occurrence and evolution of lens proteins during embryonic development between different animal classes. In all birds examined, the first and dominating lens protein (FISC), was followed by a gradual appearance of other protein fractions during a long period. In fish, the most marked phenomenon was the very large proportion of low molecular weight proteins in young and embryonic lenses. In mammals, a number of antigens appeared in a relatively short period. α-Crystallin in the latter class was one of the first lens proteins, and low molecular weight proteins constituted an important part of the lens during the whole embryonic period. Slight differences in physicochemical behavior of some of the lens proteins were noticed between the embryonic and adult stages. Some morphological aspects of protein formation in the differentiating lens fibers were also discussed.