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 w... Ausführliche Beschreibung

1. Person: McMillan, Minnie
Weitere Personen: Cecka, J. Michael verfasserin; Murphy, Donal B. verfasserin; McDevitt, Hugh O. verfasserin; Hood, Leroy verfasserin
Quelle: in Proceedings of the National Academy of Sciences of the United States of America Vol. 74, No. 11 (1977), p. 5135-5139
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Format: Online-Artikel
Sprache: English
Veröffentlicht: 1977
Beschreibung: Online-Ressource
Schlagworte: research-article
Immunology
H-2 complex gene products
Immunoprecipitation
Microsequence analysis
Sequence homology
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Zusammenfassung: 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 α 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.
ISSN: 0027-8424

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