title: Comparative study on the structure of the light chains of human immunoglobulins. II. Assignment of a new subgroup.
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.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001536:Bence Jones Protein / Q000652:urine; D001666:Binding Sites, Antibody; D003488:Cyanogen Bromide; D006801:Humans; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D007147:Immunoglobulin Light Chains / Q000652:urine; D007135:Immunoglobulin Variable Region; D009101:Multiple Myeloma / Q000276:immunology; D010446:Peptide Fragments / Q000032:analysis
chemical_list: D000596:Amino Acids; D007147:Immunoglobulin Light Chains; D007135:Immunoglobulin Variable Region; D010446:Peptide Fragments; D001536:Bence Jones Protein; D003488:Cyanogen Bromide