| Autor: |
Griess GA, Zigman S, Yulo T |
| Jazyk: |
angličtina |
| Zdroj: |
Molecular and cellular biochemistry [Mol Cell Biochem] 1976 Jul 30; Vol. 12 (1), pp. 9-14. |
| DOI: |
10.1007/BF01731898 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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