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Proteins associated with the membrane surface of lens fiber cells |
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| Authors: | Gary A. Griess Seymour Zigman |
| Affiliation: | 1. Department of Ophthalmology, University of Rochester School of Medicine and Dentistry, 601 Elmwood Avenue, Rochester, New York 14642, U.S.A.;2. Department of Biochemistry, University of Rochester School of Medicine and Dentistry, 601 Elmwood Avenue, Rochester, New York 14642, U.S.A. |
| Abstract: | The urea-soluble proteins (USP) from dogfish lenses were studied by high-resolution analytic methods. Immunoprecipitates were dissolved and analyzed in 8 m-urea-Tris-glycine buffer by polyacrylamide gel electrophoresis. All USP components were found to have properties in common with the water-soluble lens proteins (WSP) as characterized by Ferguson plots. Water-soluble lens proteins showed a preferential affinity for the isolated membrane ghosts of lens and red blood cells. Species differences are noted which may be related to species-specific functional requirements of the lens. |
| Keywords: | proteins lens crystallins albuminoid immunochemistry electrophoresis membrane absorption |
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