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HARRY MAISEL, MD; M. GOODMAN, PhD

Arch Ophthalmol. 1964;71(5):671-675.

	Since this article does not have an abstract, we have provided the first 150 words of the full text PDF and any section headings.

Introduction

Since the initial report by Mörner¹ that the soluble proteins of the lens consist of three fractions, -, β-, and -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.^4,5

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.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 . . . [Full Text PDF of this Article]

Author Affiliations
Detroit

Department of Anatomy, Wayne State University.

Footnotes
Submitted for publication Oct 14, 1963.

Supported by grant-in-aid G-261 from the National Council to Combat Blindness, Inc., New York, and by research grant GM 10634-01 from the National Institutes of Health.

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