| Autor: |
Burnett, Paul R., Eylar, E.H. |
| Zdroj: |
Journal of Biological Chemistry; May 1971, Vol. 246 Issue: 10 p3425-3430, 6p |
| Abstrakt: |
The single tryptophan residue of the basic A1 protein from bovine and human central nervous system myelin was selectively modified to the oxindole derivative with a mild oxidizing reagent BNPS-skatole, a bromine adduct of 2-(2-nitrophenylsulfenyl)-3-methylindole. Quantitative oxidation of the tryptophan residue was shown by several methods. Following reduction, no other residue appeared to be modified. The oxidized A1 protein showed the same encephalitogenic activity, antigenic specificity, and delayed-type skin reactivity as the unmodified A1 protein, thus demonstrating that position 2 of the indole ring is not critical for induction of experimental allergic encephalomyelitis in guinea pigs. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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