Analysis of Mammalian Lens Proteins by Electrophoresis

Abstract

Introduction Since the initial report by Mörner¹that 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 Manski²et al detected ten components in vertebrate lenses by using immunoelectrophoresis, while François³et 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.^4,5 In 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.⁶This 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