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Quantitative aspects of antigen-antibody reactions. II. Some comparisons between the theory and the experimental results

Published online by Cambridge University Press:  15 May 2009

Torsten Teorell
Torsten Teorell
Affiliation:
From the Institute of Physiology, University of Uppsala, Uppsala, Sweden
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The quantitative theory for the interaction between antigen and antibody presented in the previous paper has been compared with some experimental precipitin reactions published in the literature. These reactions include Type VIII pneumococcus polysaccharide-homologous (horse) antibody, egg albumin-(rabbit) anti-egg albumin and diphtheria toxin-(horse) antitoxin.

1. The general course of the experimental precipitation curves (total amount of precipitate, amounts of precipitated antigen and antibody) corresponded well to the theoretical type curves. Hence it may be concluded that the precipitates may be composed of mixtures of compounds of the types AG, A2G, A3G, …, ANG in accordance with the law of mass action. In the cases with ‘inhibition zones’, however, AG, or ANG, or both (and perhaps several more compounds) retain the same solubility as the free antigen (G) and free antibody (A).

2. With regard to the location of the ‘equivalence zones’, experiment and theory also showed a satisfactory agreement.

3. A hypothesis on the velocity of flocculation in the precipitin reaction is presented and compared with some recent results. The relation between the immunological concepts ‘equivalence (neutral) point’, ‘optimum point’ and ‘maximum precipitation point’ is also discussed.

Type
Research Article
Information
Journal of Hygiene , Volume 44 , Issue 4 , January 1946 , pp. 237 - 242
Copyright
Copyright © Cambridge University Press 1946

References

Boyd, W. C. (1941). J. Exp. Med. 74, 369.CrossRefGoogle Scholar
Culbertson, J. T. (1932). J. Immunol. 23, 439.Google Scholar
Dean, & Webb, (1926). J. Path. Bact. 29, 473.Google Scholar
Haurowitz, F. (1939). Chemie der Antigene und der Antikörper, p. 19. Fortschritte der Allergielehre, ed. by P., Kallós, Basel. New York.Google Scholar
Haurowitz, F. (1943). Schweiz. Med. Wschr. 73, 264.Google Scholar
Healey, H. & Pinfield, S. (1935). Brit. J. Exp. Path. 16, 535.Google Scholar
Heidelberger, M. (1938). J. Amer. Chem. Soc. 60, 242.CrossRefGoogle Scholar
Heidelberger, M., Kabat, E. A. & Shrivastava, D. L. (1937). J. Exp. Med. 65, 487.CrossRefGoogle Scholar
Heidelberger, M. & Kendall, F. E. (1935 a). J. Exp. Med. 61, 559.Google Scholar
Heidelberger, M. & Kendall, F. E. (1935 b). J. Exp. Med. 62, 467.Google Scholar
Heidelberger, M. & Kendall, F. E. (1935 c). J. Exp. Med. 62, 697.CrossRefGoogle Scholar
Heidelberger, M., Treffers, M. P. & Mayer, M. (1940). J. Exp. Med. 71, 277.CrossRefGoogle Scholar
Hekshey, A. D. (1941). J. Immunol. 42, 455.Google Scholar
Hooker, S. B. & Boyd, W. C. (1935). J. Gen. Physiol. 19, 373.Google Scholar
Marrack, J. R. (1938). The Chemistry of Antigens and Antibodies. London: Medical Research Council.Google Scholar
Marrack, J. R. (1942). Immunochemistry. Ann. Rev. Biochem. 11, 629.Google Scholar
Pappenheimer, A. M. (1940). J. Exp. Med. 71, 263.Google Scholar
Pappenheimer, A. M., Lundgren, H. P. & Williams, J. W. (1940). J. Exp. Med. 71, 247.CrossRefGoogle Scholar
Pappenheimer, A. M. & Robinson, E. S. (1937). J. Immunol. 32, 291.CrossRefGoogle Scholar
von Smoluchowski, (1918). Z. phys. Chem. 92, 137.Google Scholar
Taylor, G. L., Adair, G. S. & Adair, M. E. (1934). J. Hyg., Camb., 34, 118.Google Scholar
Teorell, T. (1943). Nature, Lond., 151, 696.CrossRefGoogle Scholar
Teorell, T. (1946). J. Hyg., Camb., 44, 227.Google Scholar