Analysis of Mammalian Lens Proteins by Electrophoresis
- 1 May 1964
- journal article
- research article
- Published by American Medical Association (AMA) in Archives of Ophthalmology (1950)
- Vol. 71 (5) , 671-675
- https://doi.org/10.1001/archopht.1964.00970010687014
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 sacrificingKeywords
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