| Autor: |
Moore BW; Washington University School of Medicine, Department of Psychiatry, St. Louis, MO 63110., Joy W |
| Jazyk: |
angličtina |
| Zdroj: |
Neurochemical research [Neurochem Res] 1988 Jun; Vol. 13 (6), pp. 561-5. |
| DOI: |
10.1007/BF00973298 |
| Abstrakt: |
The S-100 nervous system protein was purified from bovine and rat brains by a modification of the original procedure. The main modification consisted in substituting a step of calcium-dependent binding of S-100 to a phenyl-Sepharose column for the original step of chromatography on G-200 Sephadex. The proteins were pure as determined by SDS gel electrophoresis. HPLC on a reversed phase and on a size-separation column, and by immunological criteria. The bovine S-100 behaved as previously described, during calcium binding, by displaying a conformational change as evidenced by increase in native fluorescence. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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