التفاصيل البيبلوغرافية
| العنوان: |
Multiple Antigenic Sites on an Eicosapeptide I. PRECIPITIN STUDIES IN THE GOAT. |
| المؤلفون: |
Lieu, T.1, Chapman, G.1, Doscher, M. S.1, Mikorywak, C. A.1, Brown, R. K.1, Kong, Y. M.2 |
| المصدر: |
Immunology. Dec75, Vol. 29 Issue 6, p1133-1143. 11p. |
| مصطلحات موضوعية: |
*ANTIGENS, *BINDING sites, *PEPTIDES, *PRECIPITIN reaction, *ANTIGEN-antibody reactions, *RIBONUCLEASES |
| مستخلص: |
Purified peptide 105-124, an antigenic determinant from the carboxy terminus of ribonuclease, was found to form an immune precipitate with antibody to that region prepared by affinity chromatography from goat hyperimmune anti- serum to reduced carboxymethylated ribonuclease (CM-RNase). CM-RNase also gave an immune precipitate with the antibody. Purified antibody to another region of similar size (40-61) did not form a precipitate with CM-RNase but did co-precipitate in the presence of antibody to peptide 105-124 and CM-RNase. The precipitin reaction between antibody to peptide 105-124 and CM-RNase was inhibited by two synthetic derivatives, peptides 118-124 and ala 114-RNase 114- 124. Stoichiometry of the precipitin reactions of antibody to 105-124 with CM- RNase or peptide 105-124 suggested an antigen valency of three or more. Consistent with this both peptides 105-124 and 114-RNase 114-124 elicited immediate cutaneous reactions but 118-124 did not. These findings suggest that the eicosapeptide 105-124 is multivalent since at least three antibodies can react simultaneously with it. [ABSTRACT FROM AUTHOR] |
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