期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1986
卷号：83
期号：11
页码：3968-3971
DOI：10.1073/pnas.83.11.3968
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The binding of 125I-labeled immunogenic peptides to purified Ia molecules in detergent solution was examined by equilibrium dialysis. We used the chicken ovalbumin peptide ovalbumin-(323-339)-Tyr, which is immunogenic in the BALB/c mouse and restricted to I-Ad. 125I-labeled ovalbumin-(323-339)-Tyr was shown to bind to I-Ad but not to I-Ed, I-Ek, or I-Ak. This binding was inhibited by unlabeled ovalbumin-(323-339) but not by ovalbumin-(329-339), which is the longest N-terminally truncated peptide that fails to stimulate any of the I-Ad-restricted hybridomas that have been raised to ovalbumin-(323-339)-Tyr. As a further specificity control, we also used the chicken egg lysozyme peptide Tyr-(46-61), which has recently been studied by similar methods [Babbitt, B. P., Allen, P. M., Matsueda, G., Haber, E. & Unanue, E. R. (1985) Nature (London) 317, 359-361]. We have confirmed that it bound to I-Ak but not to I-Ek, I-Ad, or I-Ed. Thus, a specific interaction between Ia and antigen that correlates with the major histocompatibility complex restriction was demonstrated, strongly arguing in favor of a determinant selection hypothesis for such restriction.
