Modification of calf lens crystallins as determined by Gel electrophoresis
- 1 July 1976
- journal article
- research article
- Published by Springer Nature in Molecular and Cellular Biochemistry
- Vol. 12 (1) , 9-14
- https://doi.org/10.1007/bf01731898
Abstract
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.This publication has 26 references indexed in Scilit:
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