April 1968
Volume 7, Issue 2
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Articles  |   April 1968
Starch-Gel Electrophoresis of the Soluble Lens Proteins from Normal and Galactosemic Animals
Author Affiliations
  • WILLIAM S. HOLT
    Howe Laboratory of Ophthalmology, Harvard Medical School and Massachusetts Eye and Ear Infirmary Boston, Mass.
  • JIN H. KINOSHITA
    Howe Laboratory of Ophthalmology, Harvard Medical School and Massachusetts Eye and Ear Infirmary Boston, Mass.
Investigative Ophthalmology & Visual Science April 1968, Vol.7, 169-178. doi:
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      WILLIAM S. HOLT, JIN H. KINOSHITA; Starch-Gel Electrophoresis of the Soluble Lens Proteins from Normal and Galactosemic Animals. Invest. Ophthalmol. Vis. Sci. 1968;7(2):169-178.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

The soluble proteins of normal calf, rabbit, and rat lenses have been studied by the method of starch-gel electrophoresis. The electrophoretic separations of lens homogenates are compared to those of alpha, beta, and gamma crystallins prepared by paper electrophoresis and by precipitation and gel filtration techniques. Rabbit lens solutions are separated into a total of 15 protein zones, rat lens homogenates into 16, and calf into 17. Galactose cataracts which have progressed to thestage of nuclear cataract give rise to altered electrophoretic patterns. The beta and gamma protenzones decrease in staining intensity, while the alpha zone becomes very diffuse and spread out. These changes appear consistent with those observed by other techniques. Rat lenses in the prevacuolar and vacuolar stages of galactose cataract exhibit minor but characteristic alterations of certain beta protein zones. Preliminary studies of possible mechanisms of these changes are reported.

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