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. 1971 Jun;20(6):1019–1040.

Light-scattering studies of the formation of aggregates in mixtures of antigen and antibody

John R Marrack, Conway B Richards
PMCID: PMC1455950  PMID: 5558028

Abstract

Formation of aggregates in mixtures of antigen and antibody was followed by measurement of the intensity of light scattered at 90° and of the ratio of the intensities of light scattered at 45° and 135° under varied environmental conditions—concentration, antigen/antibody ratio, temperature, concentration of neutral salts, hydrogen ion and organic solutes. We propose that the aggregation of antigen—antibody complexes is accelerated by change in the structure of antibody molecules that occurs on combination with antigen. The effect of solutes on the rate of aggregation may be due to reduction of the association constant of the combination of antigen and antibody or to inhibition of the change in structure of antibody on combination. Acceleration of the early stage of aggregation by increase of temperature is attributed to increased rate of change in the structure of antibody.

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Selected References

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

  1. ATCHLEY W. A., BHAGAVAN N. V. Inhibition of antigen-antibody reactions by aminocarboxylic acids. Science. 1962 Oct 26;138(3539):528–529. doi: 10.1126/science.138.3539.528. [DOI] [PubMed] [Google Scholar]
  2. Cathou R. E., Haber E. Structure of the antibody combining site. I. Hapten stabilization of antibody conformation. Biochemistry. 1967 Feb;6(2):513–518. doi: 10.1021/bi00854a020. [DOI] [PubMed] [Google Scholar]
  3. FARR R. S. A quantitative immunochemical measure of the primary interaction between I BSA and antibody. J Infect Dis. 1958 Nov-Dec;103(3):239–262. doi: 10.1093/infdis/103.3.239. [DOI] [PubMed] [Google Scholar]
  4. Freedman M. H., Grossberg A. L., Pressman D. Evidence for ammonium and guanidinium groups in the combining sites of anti-p-azobenzenearsonate antibodies--separation of two different populations of antibody molecules. J Biol Chem. 1968 Dec 10;243(23):6186–6195. [PubMed] [Google Scholar]
  5. GOLDBERG R. J., CAMPBELL D. H. The light-scattering properties of an antigen-antibody reaction. J Immunol. 1951 Jan;66(1):79–86. [PubMed] [Google Scholar]
  6. GOULD H. J., GILL T. J., 3rd, DOTY P. THE CONFORMATION AND HYDROGEN ION EQUILIBRIUM OF NORMAL RABBIT GAMMA-GLOBULIN. J Biol Chem. 1964 Sep;239:2842–2851. [PubMed] [Google Scholar]
  7. Grossberg A. L., Markus G., Pressman D. Change in antibody conformation induced by hapten. Proc Natl Acad Sci U S A. 1965 Sep;54(3):942–945. doi: 10.1073/pnas.54.3.942. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. HABER E. RECOVERY OF ANTIGENIC SPECIFICITY AFTER DENATURATION AND COMPLETE REDUCTION OF DISULFIDES IN A PAPAIN FRAGMENT OF ANTIBODY. Proc Natl Acad Sci U S A. 1964 Oct;52:1099–1106. doi: 10.1073/pnas.52.4.1099. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. HAWKINS J. D. SOME STUDIES ON THE PRECIPITIN REACTION USING A TURBIDIMETRIC METHOD. Immunology. 1964 May;7:229–238. [PMC free article] [PubMed] [Google Scholar]
  10. Hawkins J. D. The effect of some solutes on the velocity of the precipitin reaction. Immunology. 1965 Aug;9(2):107–117. [PMC free article] [PubMed] [Google Scholar]
  11. Henney C. S., Ishizaka K. Studies on the immunogenicity of antigen-antibody precipitates. 1. The suppressive effect of anti-L and anti-H chain antibodies on the immunogenicity of human gammaG globulin. J Immunol. 1968 Nov;101(5):896–904. [PubMed] [Google Scholar]
  12. Henney C. S., Stanworth D. R. Effect of antigen on the structural configuration of homologous antibody following antigen-antibody combination. Nature. 1966 Jun 4;210(5040):1071–1072. doi: 10.1038/2101071a0. [DOI] [PubMed] [Google Scholar]
  13. Henney C. S., Stanworth D. R., Gell P. G. Demonstration of the exposure of new antigenic determinants following antigen-antibody combination. Nature. 1965 Mar 13;205(976):1079–1081. doi: 10.1038/2051079a0. [DOI] [PubMed] [Google Scholar]
  14. Herskovits T. T., Jaillet H. Structural stability and solvent denaturation of myoglobin. Science. 1969 Jan 17;163(3864):282–285. doi: 10.1126/science.163.3864.282. [DOI] [PubMed] [Google Scholar]
  15. Kekwick R. A. The serum proteins in multiple myelomatosis. Biochem J. 1940 Sep;34(8-9):1248–1257. doi: 10.1042/bj0341248. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. MARRACK J. R., GRANT R. A. The interaction of antigens and antibodies in the presence of low concentrations of salt. Br J Exp Pathol. 1953 Jun;34(3):263–272. [PMC free article] [PubMed] [Google Scholar]
  17. MARRACK J. R., ORLANS E. S. The effects of acetylation of amino groups on the reactions of antigens and antibodies. Br J Exp Pathol. 1954 Aug;35(4):389–401. [PMC free article] [PubMed] [Google Scholar]
  18. MARRACK J. R. The relation of the rates of flocculation and amounts of precipitate in precipitin reactions to the concentration of hydrogen ion and of neutral salts. Immunology. 1958 Jul;1(3):251–267. [PMC free article] [PubMed] [Google Scholar]
  19. NOZAKI Y., TANFORD C. THE SOLUBILITY OF AMINO ACIDS AND RELATED COMPOUNDS IN AQUEOUS UREA SOLUTIONS. J Biol Chem. 1963 Dec;238:4074–4081. [PubMed] [Google Scholar]
  20. PRESSMAN D., NISONOFF A., RADZIMSKI G. Specific anion effects with antibenzoate antibody. J Immunol. 1961 Jan;86:35–41. [PubMed] [Google Scholar]
  21. ROBINSON D. R., JENCKS W. P. THE EFFECT OF COMPOUNDS OF THE UREA-GUANIDINIUM CLASS ON THE ACTIVITY COEFFICIENT OF ACETYLTETRAGLYCINE ETHYL ESTER AND RELATED COMPOUNDS. J Am Chem Soc. 1965 Jun 5;87:2462–2470. doi: 10.1021/ja01089a028. [DOI] [PubMed] [Google Scholar]
  22. SINGER S. J. Physical-chemical studies on the nature of antigen-antibody reactions. J Cell Physiol Suppl. 1957 Dec;50(Suppl 1):51–78. doi: 10.1002/jcp.1030500405. [DOI] [PubMed] [Google Scholar]
  23. Tengerdy R. P. Reaction kinetic studies of the antigen antibody reactions. J Immunol. 1967 Jul;99(1):126–132. [PubMed] [Google Scholar]
  24. WINKLER M., DOTY P. Some observations on the configuration and precipitating activity of antibodies. Biochim Biophys Acta. 1961 Dec 23;54:448–454. doi: 10.1016/0006-3002(61)90084-1. [DOI] [PubMed] [Google Scholar]
  25. Warren J. C., Cheatum S. G. Effect of neutral salts on enzyme activity and structure. Biochemistry. 1966 May;5(5):1702–1707. doi: 10.1021/bi00869a036. [DOI] [PubMed] [Google Scholar]
  26. Warren J. C., Stowring L., Morales M. F. The effect of structure-disrupting ions on the activity of myosin and other enzymes. J Biol Chem. 1966 Jan 25;241(2):309–316. [PubMed] [Google Scholar]
  27. Wold R. T., Reid R. T., Farr R. S. The effect of epsilon-aminocaproic acid on antigen-antibody reactions. J Immunol. 1967 Oct;99(4):797–802. [PubMed] [Google Scholar]

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