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The formation of precipitates on mixing anti-horse sera

Published online by Cambridge University Press:  15 May 2009

G. R. E. Naylor
Affiliation:
Department of Pathology, University of Cambridge
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1. Five anto-horse sera which did not contain antibodies for horse-serum crystalbumin have been shown by absorption experiments to contain horse-serum crystalbumin.

2. All five sera precipitated when mixes with other anti-horse sera containing anti-crystalbumin, precipitation being due to the presence of horse-serum crystalbumin in one antiserum and of anti-crystalbumin in the other.

3. Antigen and its homologous antibody were never found together in the serum of an animal, and contradictory results in other experiments are probably due to impure multiple antigens.

4. It is concluded that anti-horse sera may contain some of the antigenic components of injected horse serum together with antibodies to other antigens of the horse serum, but not homologous antigen and antibody. Consequently, the ‘mutual’ precipitation of anti-horse sera is due to the presence of a number of antigens in horse serum, one or more of which, present in one anti-horse serum, in the absence of its homologous antibody, may precipitate when mixed with another anti-horse serum which contains the homologous antibody.

5. The use in these experiments of a single α-procedure optimum as the indicator of an antigen-antibody reaction illustrates a method enabling the investigation of problems involving single antigen-antibody reactions, even though the available reagents consist of mistures of antigens and mixtures of antibodies.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1950

References

REFERENCES

Ascoli, M. (1902). Zur kenntnis der präzipitinwirkung and der Eiseisskörper des Blutserums. Münch. med W schr. 49, 1409.Google Scholar
Bayne-Jones, S. (1917). Equilibria in precipitin reactions. The coexistence of a single free antigen and its antibody in the same serum. J. exp. Med. 25, 837.Google Scholar
Culbertson, J. T. (1935). The role of the precipitin antibody in the removal of intravenously injected antigen. J. Immunol. 28, 279.Google Scholar
Dean, H. R. & Webb, R. A. (1926). The influence of optimal proportions of antigen and antibody in the serum precipitation reaction. J. Path. Bact. 29, 473.Google Scholar
Dean, H. R. & Webb, R. A. (1928). The determination of the rate of antibody (precipttin) production in rabbit's blood by the method of ‘optimal proportions’. J. Path. Bact. 31, 89.Google Scholar
Duncan, J. T. (1932). The use of equivalent proportions of antigen and serum in absorption of precipitin. Brit. J. exp. Path. 13, 489.Google Scholar
Von Dungern, F. (1903). Bindungsverhältnisse bei der präzipitireaktion. Zbl. Bakt. Orig. 34, 355.Google Scholar
Eisenberg, P. (1902). Untersuchungen über spezifische präcipitaionsvorgänge. Teil I. Zbl. Bakt. Orig. 31, 773.Google Scholar
Gay, F. P. & Rusk, G. Y. (1912). The persistence of a soluble antigen in the serum of immunized rabbits. Univ. calif. Publ. Path. 2, 59.Google Scholar
Glenny, A. T. & Hopkins, B. E. (1922). Duration of passive immunity. Part I. J. Hyg., Camb., 21, 142.Google ScholarPubMed
Glenny, A. T. & Hopkins, B. E. (1923). Duration of passive immunity. Part IV. J. Hyg., Camb., 22, 208.Google ScholarPubMed
Goldsworthy, N. E. (1928). The occurrence of multiple zones in the serum precipitation reaction. J. Path. Bact. 31, 525.Google Scholar
Goldsworthy, N. E. & Rudd, G. V. (1935). Complexity of antigens in relation to zones in the precipitation reaction. J. Path. Bact. 40, 169.Google Scholar
Heidelberger, M. (1939). Quantitative absolute methods in the study of antigen-antibody reactions. Bact. Rev. 3, 49.Google Scholar
Hektoen, L. & Welker, W. H. (1925). Precipitin reactions of serum proteins. J. infect. Dis., 35, 295.Google Scholar
Hewitt, L. F. (1938). Preparation and properties of a globulin present in the albumin fraction of serum. Biochem. J., 32, 26.CrossRefGoogle ScholarPubMed
Hooker, S. B. & Boyd, W. C. (1936). The existence of antigenic determinants of diverse specificity in a single protein. III. Further notes on crystalline hen- and duck-oval-bumins. J. Immunol. 30, 41.Google Scholar
Ionesco-Mihaiesti, C. (1911). sur la coexistence de I'antigène et de I'anticorps dans le séerum des lapins préparés avec le sérum de cheval. C.R.Soc. Biol. Paris., 70, 429.Google Scholar
Kendall, F. E. (1937). Studies of serum proteins. J. Clin. Invest. 16, 921.CrossRefGoogle ScholarPubMed
Landsteiner, K. (1946). The Specificity of Serological Reactions. Revised edition. Cambridge, Mass: Harvard University Press.Google Scholar
Linossier, G. & Lemoine, G. H. (1902). Sur les substances précipitantes des albumines (Précipitines) contenues dans certains sérums spécifiques. C. R. Soc. Biol. Paris., 54, 85.Google Scholar
Naylor, G. R. E. (1948). Some observations on the reaction between horse serum and a pool of rabbit anti-horse serum. I. J. Hyg., Camb., 46, 129.CrossRefGoogle Scholar
Naylor, G. R. E. (1950). Some observation on the reaction between horse serum and a pool of rabbit anti-horse serum. II. J. Hyg., Camb. (in the Press).Google Scholar
Opie, E. L. (1923 a). The relation of antigen to antibody (precipitin) in vitro. J. Immunol., 8, 19.Google Scholar
Opie, E. L. (1923 b). The relation of antigen to antibody (precipitin) in the circulating blood. J. Immunol. 8, 55.Google Scholar
pappenheimer, A. M. (1940). Anti-egg albumin antibody in the horse. J. exp. Med. 71, 263.Google ScholarPubMed
Sørensen, S. P. L. (1925). protenis, pp. 40 et seq. Lectures given in the United states of America in 1924. Published by the Fleischmann Company.Google Scholar
Sørensen, S. P. L. (1930). The constitution of soluble proteins. C. R. Lab. Carlsberg, 18, 5, 1.Google Scholar
Taylor, G. L. (1935). The demonstration of the increase of globulin in diphtheria antitoxins by the precipitation reaction. J. Hyg., Camb., 35, 174.CrossRefGoogle ScholarPubMed
Taylor, G. L., Adair, G. S. & Adair, M. E. (1932). The estimation of proteins by the precipitation reaction. J. Hyg., Camb., 32, 340.Google ScholarPubMed
Taylor, G. L., Adair, G. S. & Adair, M. E. (1934). The precipitation reaction. Optimal proportions, neutrality and maximal precipitation in mixtures of albumin and anti-serum. J. Hyg., Camb., 34, 118.Google Scholar
Uhlenhuth, P. & Weidanz, (1909). Quoted by Uhlenhuth P. & seiffert W. (1928). Hand-buch der pathogenen Mikroorganismen, 3, 421 et seq. Founded by W. Kolle and A. V. Wassermann. Edited by W. Kolle, R. Kraus and P. Uhlenhuth.Google Scholar
Weil, R. (1916). Studies in anaphylaxis. XV. Equilibrium in precipitation reactions. Equilibrium in combination. J. Immunol. 1, 19.CrossRefGoogle Scholar
Zinsser, H. (1923). Infection and Resistance, 3rd ed. New York: Macmillan Company.Google Scholar
Zinsser, H. & Young, S. W. (1913). On the possible importance of colloidal protection in certain phases of the precipitin reaction. J. exp. Med. 17, 396.Google Scholar