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Published November 1, 1977 | public
Journal Article Open

Structure of murine Ia antigens: Partial NH2-terminal amino acid sequences of products of the I-E or I-C subregion


Partial amino acid sequences of the Ia molecule encoded by the I-E or I-C (I-EC) subregion of the major histocompatibility complex of the mouse are presented. The Ia molecule appears to be comprised of two noncovalently associated polypeptides. The larger subunit, α, has an approximate molecular weight of 35,000 and the smaller subunit, β , an approximate molecular weight of 28,000. Several interesting homology relationships (or the lack thereof) are apparent when the Ia polypeptides from the I-EC subregion are compared both with their counterparts from man and guinea pig and with the molecules encoded in the I-A subregion. Clearly the most impressive homology relationship is that seen between the polypeptide from the I-EC subregion of mouse and its human counterpart. This is in striking contrast to the β polypeptide, which bears no apparent homology to its human counterpart.

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© 1977 by the National Academy of Sciences. Contributed by Hugh O. McDevitt, August 31, 1977. M.M. is a Senior Gosney Fellow (California Institute of Technology). J.M.C. is supported by National Institutes of Health Fellowship A105276. D.B.M. is a Fellow of the Cancer Research Institute. This work was supported by Grants AI10781, GM06965 and AI07757 from the National Institutes of Health. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.


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