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Article
May 1964

Analysis of Mammalian Lens Proteins by Electrophoresis

Author Affiliations

Detroit
Department of Anatomy, Wayne State University.

Arch Ophthalmol. 1964;71(5):671-675. doi:10.1001/archopht.1964.00970010687014
Abstract

Introduction  Since the initial report by Mörner1 that the soluble proteins of the lens consist of three fractions, α-, β-, and γ-crystallins, many attempts have been made to obtain a definitive fractionation of lens proteins, using a variety of techniques. Thus Manski2 et al detected ten components in vertebrate lenses by using immunoelectrophoresis, while François3 et al noted 12-16 fractions in the lens of different species, by means of high-tension microelectrophoresis in agar. Chromatographic analyses have yielded ten fractions.4,5In the present study lens proteins were analyzed by two-dimensional starch gel electrophoresis, a technique which has been effectively applied for the resolution of serum proteins.6 This method has distinct advantages when used for the study of a heterogeneous collection of proteins, since their separation in starch is dependent on both molecular size and electrophoretic properties.

Materials and Methods 

Lens Proteins.  —Lenses obtained immediately after sacrificing

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