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Modification of calf lens crystallins as determined by Gel electrophoresis

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Summary

Variations in size and charge of calf lens proteins, particularly gamma crystallins, were studied by polyacrylamide gel electrophoresis. Exposure of gamma crystallins to near-UV light in the presence of L-tryptophan produces species of higher electrophoretic mobility and higher retardation. Treatment with urea and sulfonation also produced changes in the retardation co-efficient. The increase of retardation co-efficient of gamma crystallin is interpreted to be a result of conformational changes. Gamma crystallins are particularly sensitive to photo-modification, and this process may be associated with age-related changes in the lens.

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Authors and Affiliations

  1. Departments of Surgery (Ophthalmology) and Biochemistry, University of Rochester School of Medicine and Dentistry, 601 Elmwood Avenue, 14642, Rochester, New York, USA

    Gary A. Griess Ph.D., Seymour Zigman Ph.D. & Teresa Yulo

Authors
  1. Gary A. Griess Ph.D.
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  2. Seymour Zigman Ph.D.
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  3. Teresa Yulo
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Additional information

Supported by research grants from the U.S.P.H.S. EY #00459, a FIGHT-FOR-SIGHT Postdoctoral Research Fellowship (FIGHT-FOR-SIGHT, INC., N.Y.C.) and The Rochester Eye and Human Parts Bank, Inc.

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Griess, G.A., Zigman, S. & Yulo, T. Modification of calf lens crystallins as determined by Gel electrophoresis. Mol Cell Biochem 12, 9–14 (1976). https://doi.org/10.1007/BF01731898

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  • DOI: https://doi.org/10.1007/BF01731898

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