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. 1977 Nov;74(11):5135–5139. doi: 10.1073/pnas.74.11.5135

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

M McMillan, J M Cecka, D B Murphy, H O McDevitt, L Hood
PMCID: PMC432115  PMID: 270750

Abstract

Partial amino acid sequence 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, alpha, has an approximate molecular weight of 35,000 and the smaller subunit, beta, 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 alpha polypeptide from the I-EC subregion of mouse and its human counterpart. This is in striking contrast to the beta polypeptide, which bears no apparent homology to its human counterpart.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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