Comparative study on the structure of the light chains of human immunoglobulins. II. Assignment of a new subgroup

J Biochem. 1979 Nov;86(5):1523-35. doi: 10.1093/oxfordjournals.jbchem.a132670.

Abstract

The primary structure of the variable region of the human lambda type Bence Jones protein NIG-48 was determined by analysis of the N-terminal sequence of the completely reduced and aminoethylated protein, as well as of five cyanogen bromide fragments. The variable region of NIG-48 contains 112 amino acid residues. The protein NIG-48, having a unique sequence of the variable region, a low degree of homology (about 50%) with lambda chains of the five other subgroups and the addition of two residues around 65, may represent a new subgroup, namely V lambda VI.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Bence Jones Protein* / urine
  • Binding Sites, Antibody*
  • Cyanogen Bromide
  • Humans
  • Immunodiffusion
  • Immunoelectrophoresis
  • Immunoglobulin Light Chains* / urine
  • Immunoglobulin Variable Region*
  • Multiple Myeloma / immunology
  • Peptide Fragments / analysis

Substances

  • Amino Acids
  • Immunoglobulin Light Chains
  • Immunoglobulin Variable Region
  • Peptide Fragments
  • Bence Jones Protein
  • Cyanogen Bromide