Allotypically related sequences in the Fd fragment of rabbit immunoglobulin heavy chains

Biochem J. 1971 Sep;124(2):301-18. doi: 10.1042/bj1240301.

Abstract

The sequence has been completed of the N-terminal 94 residues of the variable section of the Fd fragment of heavy chains from rabbit immunoglobulin G (IgG) of allotype As1. Most of the sequence of the same section from IgG of allotype Aa3 is also reported. These results, in conjunction with a substantial sequence of the variable region of allotype Aa2 reported elsewhere (Fleischman, 1971), show the presence of 16 positions (including six consecutive positions) in which the residue present correlates with the allotype. No allotype-related sequence variation has been found in the constant section of the Fd fragment. This evidence supports the view that two genes code for the heavy chain and it can be used as evidence in favour of somatic mutation as the origin of the variability in the sequence of the N-terminal section. The evolutionary origin of the ;a' locus allotypes of rabbit immunoglobulins remains obscure.

MeSH terms

  • Amino Acid Sequence*
  • Amino Acids / analysis
  • Animals
  • Antigens
  • Carbon Isotopes
  • Chromatography
  • Chymotrypsin
  • Electrophoresis
  • Hydrogen-Ion Concentration
  • Immunoglobulin G / analysis
  • Immunoglobulins / analysis*
  • Molecular Biology
  • Papain
  • Peptides / analysis
  • Peptides / isolation & purification
  • Rabbits
  • Trypsin

Substances

  • Amino Acids
  • Antigens
  • Carbon Isotopes
  • Immunoglobulin G
  • Immunoglobulins
  • Peptides
  • Chymotrypsin
  • Trypsin
  • Papain