Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1976 Dec;73(12):4471–4473. doi: 10.1073/pnas.73.12.4471

Some correlations between specificity and sequence of the first complementarity-determining segments of human kappa light chains.

E A Kabat, T T Wu, H Bilofsky
PMCID: PMC431504  PMID: 826908

Abstract

Examination of the sequences of the first complementarity-determining segments of the light chains of two IgM cold agglutinins agains blood group I, four monoclonal IgM antibodies against IgG proteins, and of three Bence Jones proteins provides clues for predicting which residues contribute to antibody specificity and indicates that these predictions may be tested by evaluating recovery of antibody activity and specificity when various light chains are recombined with homologous and heterologous heavy chains.

Full text

PDF
4472

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Capra J. D., Kehoe J. M. Hypervariable regions, idiotypy, and the antibody-combining site. Adv Immunol. 1975;20:1–40. doi: 10.1016/s0065-2776(08)60205-9. [DOI] [PubMed] [Google Scholar]
  2. Capra J. D., Kehoe J. M., Williams R. C., Jr, Feizi T., Kunkel H. G. Light chain sequences of human IgM cold agglutinins (variable-region subgroups amino-acid sequence-kappa light chain-N-terminal). Proc Natl Acad Sci U S A. 1972 Jan;69(1):40–43. doi: 10.1073/pnas.69.1.40. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Capra J. D., Kehoe J. M., Winchester R. J., Kunkel H. G. Structure-function relationships among anti-gamma globulin antibodies. Ann N Y Acad Sci. 1971 Dec 31;190:371–381. doi: 10.1111/j.1749-6632.1971.tb13549.x. [DOI] [PubMed] [Google Scholar]
  4. Davies D. R., Padlan E. A., Segal D. M. Three-dimensional structure of immunoglobulins. Annu Rev Biochem. 1975;44:639–667. doi: 10.1146/annurev.bi.44.070175.003231. [DOI] [PubMed] [Google Scholar]
  5. Epp O., Colman P., Fehlhammer H., Bode W., Schiffer M., Huber R., Palm W. Crystal and molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI. Eur J Biochem. 1974 Jun 15;45(2):513–524. doi: 10.1111/j.1432-1033.1974.tb03576.x. [DOI] [PubMed] [Google Scholar]
  6. Fehlhammer H., Schiffer M., Epp O., Colman P. M., Lattman E. E., Schwager P., Steigemann W., Schramm H. J. The structure determination of the variable portion of the Bence-Jones protein Au. Biophys Struct Mech. 1975 Feb 19;1(2):139–146. doi: 10.1007/BF00539775. [DOI] [PubMed] [Google Scholar]
  7. Feizi T., Kabat E. A., Vicari G., Anderson B., Marsh W. L. Immunochemical studies on blood groups.XLIX. The I antigen complex: specificity differences among anti-I sera revealed by quantitative precipitin studies; partial structure of the I determinant specific for one anti-I serum. J Immunol. 1971 Jun;106(6):1578–1592. [PubMed] [Google Scholar]
  8. Gergely J., Wang A. C., Fudenberg H. H. Chemical analyses of variable regions of heavy and light chains of cold agglutinins. Vox Sang. 1973 May;24(5):432–440. doi: 10.1111/j.1423-0410.1973.tb03484.x. [DOI] [PubMed] [Google Scholar]
  9. Givol D. Affinity labeling and topology of the antibody combining site. Essays Biochem. 1974;10:73–103. [PubMed] [Google Scholar]
  10. Kabat E. A., Wu T. T. Attempts to locate complementarity-determining residues in the variable positions of light and heavy chains. Ann N Y Acad Sci. 1971 Dec 31;190:382–393. doi: 10.1111/j.1749-6632.1971.tb13550.x. [DOI] [PubMed] [Google Scholar]
  11. Kabat E. A., Wu T. T., Bilofsky H. Attempts to locate residues in complementarity-determining regions of antibody combining sites that make contact with antigen. Proc Natl Acad Sci U S A. 1976 Feb;73(2):617–619. doi: 10.1073/pnas.73.2.617. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kobzik L., Brown M. C., Cooper A. G. Demonstration of an idiotypic antigen on a monoclonal cold agglutinin and on its isolated heavy and light chains. Proc Natl Acad Sci U S A. 1976 May;73(5):1702–1706. doi: 10.1073/pnas.73.5.1702. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kunkel H. G., Agnello V., Joslin F. G., Winchester R. J., Capra J. D. Cross-idiotypic specificity among monoclonal IgM proteins with anti- -globulin activity. J Exp Med. 1973 Feb 1;137(2):331–342. doi: 10.1084/jem.137.2.331. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. MARCUS D. M., KABAT E. A., ROSENFIELD R. E. THE ACTION OF ENZYMES FROM CLOSTRIDIUM TERTIUM ON THE I ANTIGENIC DETERMINANT OF HUMAN ERYTHROCYTES. J Exp Med. 1963 Aug 1;118:175–194. doi: 10.1084/jem.118.2.175. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Manjula B. N., Glaudemans C. P., Mushinski E. B., Potter M. Subunit interactions in mouse myeloma proteins with anti-galactan activity. Proc Natl Acad Sci U S A. 1976 Mar;73(3):932–936. doi: 10.1073/pnas.73.3.932. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Metzger H. Characterization of a human macroglobulin. V. A Waldenström macroglobulin with antibody activity. Proc Natl Acad Sci U S A. 1967 May;57(5):1490–1497. doi: 10.1073/pnas.57.5.1490. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Poljak R. J., Amzel L. M., Chen B. L., Phizackerley R. P., Saul F. The three-dimensional structure of the fab' fragment of a human myeloma immunoglobulin at 2.0-angstrom resolution. Proc Natl Acad Sci U S A. 1974 Sep;71(9):3440–3444. doi: 10.1073/pnas.71.9.3440. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Raub W. F. The PROPHET system and resource sharing. Fed Proc. 1974 Dec;33(12):2390–2392. [PubMed] [Google Scholar]
  19. Riesen W. F., Braun D. G., Jaton J. C. Human and murine phosphorycholine-binding immunoglobulins: conserved subgroup and first hypervariable region of heavy chains. Proc Natl Acad Sci U S A. 1976 Jun;73(6):2096–2100. doi: 10.1073/pnas.73.6.2096. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Riesen W., Rudikoff S., Oriol R., Potter M. An IgM Waldenström with specificity against phosphorylcholine. Biochemistry. 1975 Mar 11;14(5):1052–1057. doi: 10.1021/bi00676a026. [DOI] [PubMed] [Google Scholar]
  21. Schiffer M., Girling R. L., Ely K. R., Edmundson A. B. Structure of a lambda-type Bence-Jones protein at 3.5-A resolution. Biochemistry. 1973 Nov 6;12(23):4620–4631. doi: 10.1021/bi00747a013. [DOI] [PubMed] [Google Scholar]
  22. Segal D. M., Padlan E. A., Cohen G. H., Rudikoff S., Potter M., Davies D. R. The three-dimensional structure of a phosphorylcholine-binding mouse immunoglobulin Fab and the nature of the antigen binding site. Proc Natl Acad Sci U S A. 1974 Nov;71(11):4298–4302. doi: 10.1073/pnas.71.11.4298. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Suter L., Barnikol H. U., Watanabe S., Hilschmann N. Die Primärstruktur einer monoklonale Immunglobulin-L-Kette der Subgruppe 3 vom kappa-Typ (Bence-Jones Protein TI) Hoppe Seylers Z Physiol Chem. 1969 Feb;350(2):275–278. [PubMed] [Google Scholar]
  24. Suter L., Barnikol H. U., Watanabe S., Hilschmann N. Zur Strukturregel der antikörper. Die Primärstruktur einer monoklonalen Immunoglobulin-L-Kette vom kappa-Typ, Subgruppe 3 (Bence-Jones-Protein Ti). IV. Die vollständige Aminosäuresequenz und ihre Bedeutung für den Mechanismus der Antikörperbildung. Hoppe Seylers Z Physiol Chem. 1972 Feb;353(2):189–208. [PubMed] [Google Scholar]
  25. Willims R. C., Jr, Kunkel H. G., Capra J. D. Antigenic specificities related to the cold agglutinin activity of gamma M globulins. Science. 1968 Jul 26;161(3839):379–381. doi: 10.1126/science.161.3839.379. [DOI] [PubMed] [Google Scholar]
  26. Wu T. T., Kabat E. A. An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementarity. J Exp Med. 1970 Aug 1;132(2):211–250. doi: 10.1084/jem.132.2.211. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Wu T. T., Kabat E. A., Bilofsky H. Similarities among hypervariable segments of immunoglobulin chains. Proc Natl Acad Sci U S A. 1975 Dec;72(12):5107–5110. doi: 10.1073/pnas.72.12.5107. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES