Structure of murine Ia antigens. Two dimensional electrophoretic analyses and high pressure liquid chromatography tryptic peptide maps of products of the I-A and I-E subregions and of an associated invariant polypeptide

J Exp Med. 1981 Apr 1;153(4):936-50. doi: 10.1084/jem.153.4.936.

Abstract

We demonstrate that an invariant polypeptide, first described by Jones et al. (21), co-immunoprecipitates with our Ia molecules, that its interaction with Ia polypeptides varies with haplotype, and that it is not a precursor of the Aalpha, Abeta, Ealpha, or Ebeta. polypeptides. We also show that the polypeptides that we have previously characterized are contaminated with very little, if any, invariant protein. Further, we have used our high-pressure liquid chromatography tryptic peptide map technique to formally map the genes encoding Aalpha, Abeta, and Ebeta to the I-A subregion using recombinant and F1 hybrid mice.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Chromatography, High Pressure Liquid
  • Chromosome Mapping
  • Electrophoresis, Polyacrylamide Gel
  • Histocompatibility Antigens Class II*
  • Isoelectric Focusing
  • Mice
  • Mice, Inbred A
  • Mice, Inbred C3H
  • Peptides* / isolation & purification
  • Phenylalanine / metabolism
  • Protein Biosynthesis*
  • Sulfur Radioisotopes
  • Tritium
  • Trypsin / pharmacology*

Substances

  • Histocompatibility Antigens Class II
  • Peptides
  • Sulfur Radioisotopes
  • Tritium
  • Phenylalanine
  • Trypsin