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
—Lenses obtained immediately after sacrificing
MAISEL H, GOODMAN M. Analysis of Mammalian Lens Proteins by Electrophoresis. Arch Ophthalmol. 1964;71(5):671–675. doi:https://doi.org/10.1001/archopht.1964.00970010687014
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