Structural studies of the protein portion of the H-2-linked Ia glycoprotein antigens of the mouse: tryptic peptide comparison of products from the I-A and I-C subregions of B10.HTT

J. H. Freed, C. S. David, D. C. Shreffler, S. G. Nathenson

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

In antigens from the I-A8 and I.C(κ) subregions of the B10.HTT (H-2(t3)) strain of mice were isolated by indirect immunoprecipitation of arginine-labeled, nonionic detergent-solubilized materials. After biochemical purification the electrophoretically homogeneous 28,000 dalton glycoprotein β chains from the Ia precipitates were digested with trypsin and the resultant radiolabeled tryptic peptides were compared by analytical ion exchange chromatography. These comparisons reveal that the β chains of Ia antigens from the A (I-A(s) and C (I-C(κ)) subregions of B10.HTT share only two out of 12 to 14 of their arginine tryptic peptides. Thus these noncross-reactive Ia antigens are structurally quite diverse, and would possess sufficient structural variability to account for their lack of antigenic cross-reactivity.

Original languageEnglish (US)
Pages (from-to)91-97
Number of pages7
JournalJournal of Immunology
Volume121
Issue number1
StatePublished - 1978
Externally publishedYes

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Histocompatibility Antigens Class II
Arginine
Glycoproteins
Peptides
Ion Exchange Chromatography
Immunoprecipitation
Detergents
Trypsin
Proteins
I-antigen

ASJC Scopus subject areas

  • Immunology

Cite this

Structural studies of the protein portion of the H-2-linked Ia glycoprotein antigens of the mouse : tryptic peptide comparison of products from the I-A and I-C subregions of B10.HTT. / Freed, J. H.; David, C. S.; Shreffler, D. C.; Nathenson, S. G.

In: Journal of Immunology, Vol. 121, No. 1, 1978, p. 91-97.

Research output: Contribution to journalArticle

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