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. 1972 Jun;22(6):1029–1036.

Dinitrophenyl-reactive immunoglobulins in the serum of normal bowfin, Amia calva

Claire Bradshaw, M M Sigel
PMCID: PMC1407871  PMID: 4624342

Abstract

The sera from unimmunized bowfin agglutinate a large variety of red cells. Although they precipitate DNP-BSA they manifest only slight agglutinating capacity for DNP-coated cells. 15S immunoglobulin isolated by DEAE-cellulose chromatography followed by Sephadex G-200 gel filtration possessed a high level of broad reactivity towards unmodified DNP-coated cells, whereas the 7S immunoglobulin isolated by this procedure was inactive. However, following precipitation of whole serum with DNP-BSA both molecules could be recovered in a form which demonstrated specificity for DNP, in that both precipitated DNP-BSA and agglutinated DNP-coated cells but not unmodified cells. The mechanism of activation of the 7S molecule is not known but the data suggest that this immunoglobulin is divalent.

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Selected References

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

  1. Bing D. H., Weyand J. G., Stavitsky A. B. Hemagglutination with aldehyde-fixed erythrocytes for assay of antigens and antibodies. Proc Soc Exp Biol Med. 1967 Apr;124(4):1166–1170. doi: 10.3181/00379727-124-31953. [DOI] [PubMed] [Google Scholar]
  2. Bradshaw C. M., Clem L. W., Sigel M. M. Immunologic and immunochemical studies on the gar, Lepisosteus platyrhincus. I. Immune responses and characterization of antibody. J Immunol. 1969 Sep;103(3):496–504. [PubMed] [Google Scholar]
  3. Brandriss M. W. Antibody-like activity to the 2,4-dinitrophenyl group in normal human sera. Nature. 1969 Mar 8;221(5184):960–962. doi: 10.1038/221960a0. [DOI] [PubMed] [Google Scholar]
  4. Clem L. W., Small P. A., Jr Phylogeny of immunoglobulin structure and function. I. Immunoglobulins of the lemon shark. J Exp Med. 1967 May 1;125(5):893–920. doi: 10.1084/jem.125.5.893. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Clem L. W., Small P. A., Jr Phylogeny of immunoglobulin structure and function. V. Valences and association constants of teleost antibodies to a haptenic determinant. J Exp Med. 1970 Sep 1;132(3):385–400. doi: 10.1084/jem.132.3.385. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. FARAH F. S., KERN M., EISEN H. N. The preparation and some properties of purified antibody specific for the 2,4-dinitrophenyl group. J Exp Med. 1960 Dec 1;112:1195–1210. doi: 10.1084/jem.112.6.1195. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Haimovich J., Sela M., Dewdney J. M., Batchelor F. R. Anti-penicilloyl antibodies: detection with penicilloylated bacteriophage and isolation with a specific immunoadsorbent. Nature. 1967 Jun 24;214(5095):1369–1370. doi: 10.1038/2141369a0. [DOI] [PubMed] [Google Scholar]
  8. Koshland D. E., Jr, Neet K. E. The catalytic and regulatory properties of enzymes. Annu Rev Biochem. 1968;37:359–410. doi: 10.1146/annurev.bi.37.070168.002043. [DOI] [PubMed] [Google Scholar]
  9. Leslie G. A., Clem L. W. Production of anti-hapten antibodies by several classes of lower vertebrates. J Immunol. 1969 Sep;103(3):613–617. [PubMed] [Google Scholar]
  10. Leslie G. A., Clem L. W. Reactivity of normal shark immunoglobulins with nitrophenyl ligands. J Immunol. 1970 Dec;105(6):1547–1552. [PubMed] [Google Scholar]
  11. Litman G. W., Frommel D., Finstad J., Good R. A. The evolution of the immune reponse. IX. Immunoglobulins of the bowfin: purification and characterization. J Immunol. 1971 Mar;106(3):747–754. [PubMed] [Google Scholar]
  12. Mäkelä O. Assay of anti-hapten antibody with the aid of hapten-coupled bacteriophage. Immunology. 1966 Jan;10(1):81–86. [PMC free article] [PubMed] [Google Scholar]
  13. Rudikoff S., Voss E. W., Sigel M. M. Biological and chemical properties of natural antibodies in the nurse shark. J Immunol. 1970 Dec;105(6):1344–1352. [PubMed] [Google Scholar]
  14. SCHACHMAN H. K. THE ULTRACENTRIFUGE: PROBLEMS AND PROSPECTS. Biochemistry. 1963 Sep-Oct;2:887–905. doi: 10.1021/bi00905a001. [DOI] [PubMed] [Google Scholar]
  15. SCHEIDEGGER J. J. Une micro-méthode de l'immuno-electrophorèse. Int Arch Allergy Appl Immunol. 1955;7(2):103–110. [PubMed] [Google Scholar]
  16. Voss E. W., Jr, Rudikoff S., Sigel M. M. Comparative ligand-binding by purified nurse shark natural antibodies and anti-2,4-dinitrophenyl antibodies from other species. J Immunol. 1971 Jul;107(1):12–18. [PubMed] [Google Scholar]

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