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 journalArticlepeer-review

15 Scopus citations

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 - Dec 1 1978

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

Fingerprint Dive into the research topics of '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'. Together they form a unique fingerprint.

Cite this