Skip to main content
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
. 1973 Jan;70(1):235–239. doi: 10.1073/pnas.70.1.235

Immunochemical Analysis of the Cross-Reacting Idiotypes of Mouse Myeloma Proteins with Anti-Dextran Activity and Normal Anti-Dextran Antibody

Dennis Carson 1,2, Martin Weigert 1,2
PMCID: PMC433222  PMID: 4119224

Abstract

The idiotype of the mouse myeloma protein with anti-α-1,3 dextran activity, J558, has been characterized by a solid-phase radioimmunoassay. The idiotype of the J558 protein depends on a specific light and heavy chain interaction and is altered in the presence of the hapten, nigerose. Cross-reacting idiotypes were found on another mouse myeloma protein with α1,3 dextran specificity, normal anti-dextran antibody, and certain reconstructed myeloma proteins composed of the J558 heavy chain and heterologous light chains.

Keywords: radioimmunoassay, hapten, light and heavy chains, mice

Full text

PDF
235

Selected References

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

  1. Askenase P. W., Leonard E. J. Solid phase radioimmunoassay of human beta 1C globulin. Immunochemistry. 1970 Jan;7(1):29–41. doi: 10.1016/0019-2791(70)90028-5. [DOI] [PubMed] [Google Scholar]
  2. Blomberg B., Geckeler W. R., Weigert M. Genetics of the antibody response to dextran in mice. Science. 1972 Jul 14;177(4044):178–180. doi: 10.1126/science.177.4044.178. [DOI] [PubMed] [Google Scholar]
  3. Bridges S. H., Little J. R. Recovery of binding activity in reconstituted mouse myeloma proteins. Biochemistry. 1971 Jun 22;10(13):2525–2530. doi: 10.1021/bi00789a016. [DOI] [PubMed] [Google Scholar]
  4. Brient B. W., Nisonoff A. Quantitative investigations of idiotypic antibodies. IV. Inhibition by specific haptens of the reaction of anti-hapten antibody with its anti-idiotypic antibody. J Exp Med. 1970 Nov;132(5):951–962. doi: 10.1084/jem.132.5.951. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Carrel S., Barandun S. Protein-containing polyacrylamide gels: their use as immunoadsorbents of high capacity. Immunochemistry. 1971 Jan;8(1):39–48. doi: 10.1016/0019-2791(71)90420-4. [DOI] [PubMed] [Google Scholar]
  6. Edelman G. M., Gottlieb P. D. A genetic marker in the variable region of light chains of mouse immunoglobulins. Proc Natl Acad Sci U S A. 1970 Nov;67(3):1192–1199. doi: 10.1073/pnas.67.3.1192. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Eichmann K., Kindt T. J. The inheritance of individual antigenic specificities of rabbit antibodies to streptococcal carbohydrates. J Exp Med. 1971 Aug 1;134(2):532–552. doi: 10.1084/jem.134.2.532. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. GREENWOOD F. C., HUNTER W. M., GLOVER J. S. THE PREPARATION OF I-131-LABELLED HUMAN GROWTH HORMONE OF HIGH SPECIFIC RADIOACTIVITY. Biochem J. 1963 Oct;89:114–123. doi: 10.1042/bj0890114. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kunkel H. G. Experimental approaches tohomogenous antibody populations. iIndividual antigenic specificity, cross specificity and diversity of human antibodies. Fed Proc. 1970 Jan-Feb;29(1):55–58. [PubMed] [Google Scholar]
  10. Lundblad A., Steller R., Kabat E. A., Hirst J. W., Weigert M. G., Cohn M. Immunochemical studies on mouse myeloma proteins with specificity for dextran or for levan. Immunochemistry. 1972 May;9(5):535–544. doi: 10.1016/0019-2791(72)90063-8. [DOI] [PubMed] [Google Scholar]
  11. Potter M., Lieberman R. Common individual antigenic determinants in five of eight BALB-c IgA myeloma proteins that bind phosphoryl choline. J Exp Med. 1970 Oct 1;132(4):737–751. doi: 10.1084/jem.132.4.737. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Potter M., Lieberman R. Genetics of immunoglobulins in the mouse. Adv Immunol. 1967;7:91–145. doi: 10.1016/s0065-2776(08)60127-3. [DOI] [PubMed] [Google Scholar]
  13. WILHAM C. A., ALEXANDER B. H., JEANES A. Heterogeneity in dextran preparations. Arch Biochem Biophys. 1955 Nov;59(1):61–75. doi: 10.1016/0003-9861(55)90463-x. [DOI] [PubMed] [Google Scholar]
  14. Weigert M. G., Cesari I. M., Yonkovich S. J., Cohn M. Variability in the lambda light chain sequences of mouse antibody. Nature. 1970 Dec 12;228(5276):1045–1047. doi: 10.1038/2281045a0. [DOI] [PubMed] [Google Scholar]
  15. Wofsy L., Burr B. The use of affinity chromatography for the specific purification of antibodies and antigens. J Immunol. 1969 Aug;103(2):380–382. [PubMed] [Google Scholar]
  16. 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]
  17. Young N. M., Jocius I. B., Leon M. A. Binding properties of a mouse immunoglobulin M myeloma protein with carbohydrate specificity. Biochemistry. 1971 Aug 31;10(18):3457–3460. doi: 10.1021/bi00794a022. [DOI] [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