Comparative Studies on the Structure of the Light Chains of Human Immunoglobulins. IV. Assignment of a Subsubgroup1
- 1 February 1983
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 93 (2), 421-429
- https://doi.org/10.1093/oxfordjournals.jbchem.a134196
Abstract
Amino acid sequence analysis was done on a human λ Bence Jones protein NIG-64 with the major objective of determining the sequence of the variable region. Nineteen tryptic peptides covering 216 residues were isolated from the completely reduced and aminoethylated protein, and 17 of these were completely sequenced. These comprised the entire variable region and 11 from the constant region. For the remaining peptides covering the rest of the constant region, only partial sequences or the amino acid compositions were determined. All the tryptic peptides could be arranged in order on the basis of the above results and homology with other human λ. light chains of the same isotype. The sequence of the variable region of the protein is highly homologous with that of protein New of subgroup VλI as compared with other proteins of the same subgroup, suggesting that subgroup VλI may be further divided into subsubgroups, namely subsubgroups VλI-1 and VλI-2.Keywords
This publication has 4 references indexed in Scilit:
- High-performance liquid chromatography of peptides on a macroreticular cation-exchange resin: Application to peptide mapping of Bence-Jones proteinsAnalytical Biochemistry, 1982
- Diversity of germ-line immunoglobulin VH genesNature, 1981
- A single VH gene segment encodes the immune response to phosphorylcholine: Somatic mutation is correlated with the class of the antibodyCell, 1981
- Identification and nucleotide sequence of a diversity DNA segment (D) of immunoglobulin heavy-chain genesNature, 1981