| Autor: |
E.H. Eylar, Fred C. Westall, Steven Brostoff |
| Rok vydání: |
1971 |
| Předmět: |
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| Zdroj: |
Journal of Biological Chemistry. 246:3418-3424 |
| ISSN: |
0021-9258 |
| DOI: |
10.1016/s0021-9258(18)62240-9 |
| Popis: |
A peptide (Peptide R) of 46 residues was isolated in unusually high yield (40 to 85%) from a peptic digest of the A1 protein, a basic protein from bovine myelin of the central nervous system. This peptide (4990 daltons) induced experimental allergic encephalomyelitis in rabbits but was inactive in guinea pigs and monkeys at the doses tested. In contrast, the absence of antigenic determinants to anti-A1 protein antibody in Peptide R was demonstrated by the passive hemagglutination inhibition test. It was concluded, therefore, that the encephalitogenic determinants of Peptide R plays an insignificant role in interaction with antibody. Peptide R lacks tryptophan and thereby differs from the 9-residue segment of the A1 protein which was previously shown to induce experimental allergic encephalomyelitis in guinea pigs (and rabbits). Peptides derived from the COOH-terminal portion of Peptide R were also inactive as encephalitogens in guinea pigs. Peptide R is released from the A1 protein with pepsin by hydrolysis of Phe-Phe linkages; phenylalanine thus occupies the COOH- and NH2-terminal positions. The amino acid sequence of Peptide R was determined with the Edman procedure on the six tryptic peptides: [see PDF for sequence]. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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