By Frank J. Dlxon (Ed.)
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SCHWARTZ ponder animals. It was not immunogenic by itself, but if coupled to a carrier molecule, it could elicit antibodies specific for itself. , they were unable to recognize the PLL carrier determinant. This specificity defect did not appear to be in the B cell repertoire because it could be by-passed at the antibody level by complexing the antigen to an immunogenic carrier. This observation, plus the failure to overcome the defect in DTH, suggested that the problem was located at an earlier step in the immune response, one that was essential for both DTH and antibody formation.
Disteche, C. , Ruddle, F. , Eisen, H. , and Tonegawa, S. (1985). Science 227, 941. , Mage, R. , Kelus, A. , and Rajewsky, K. J . Exp. Med. 146, 792. Krensky, A. M . , Reiss, C. , Strominger, J. , and Burakoff, S. J. J. Intmunol. 129, 2001. , Davis, M. , Early, P. W.. Hood, L. , and Watson, J. D. J. Exp. Med. 152, 1745. , Siu, C . , Kapp. J. A , , Kappler, J. , Marrack, P . , Pierce, C. , and Hood, L. J . Exp. Med. 158, 210. Kronenberg, M . , and Hood, L. (1985). Nature (London) 313, 647. , Trauheker, A,, and Tonagawa, S.
Jn working with the branched chain synthetic polypeptides, they noted that if histidine were substituted for tyrosine, to produce (H,G)-A--L instead of (T,G)-A--L, the genetic control completely reversed. The CBA mouse was shown to be a responder to (H,G)-A--L, while the C57BL mouse was shown to be a nonresponder. In subsequent experiments, when a phenylalanine was substituted for a tyrosine, (P,G)-A--L, it was found that both strains responded equally well, while if the aromatic amino acid was deleted, leav- lr G E N E S OF THE M U R I N E M H C 37 ing only glutamic acid residues attached to the DL-Ala side chains, G-A--L, then neither strain responded.