Hostname: page-component-84b7d79bbc-lrf7s Total loading time: 0 Render date: 2024-07-29T07:54:20.063Z Has data issue: false hasContentIssue false
  • English
  • Français

Electrophoretic and Immunological Studies on Sera from Calves from Birth to Weaning II. Electrophoretic and Serological Studies with Special Reference to the Normal and Induced Agglutinins to Trichomonas Foetus

Published online by Cambridge University Press:  15 May 2009

A. E. Pierce
A. E. Pierce
Affiliation:
A.R.C. Institute of Animal Physiology, Babraham, Cambridge
Rights & Permissions [Opens in a new window]

Summary

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

1. The lacto-globulin in bovine colostral whey, and the γ globulin in the serum contain the normal and induced agglutinins to the protozoon Trichomonas foetus.

2. A decline in γ globulin in sera from cattle approaching calving may be associated with the concentration of the lacto-globulin in the udder.

3. The elimination of the passive normal and induced agglutinins acquired by the neonatal calf was logarithmic. The autogenous production of γ globulin by the calf occurred soon after birth, resulting in an apparent decline in the rate of elimination of the lacto-globulins.

4. The autogenous production of γ globulin was not necessarily accompanied by that of detectable normal agglutinin.

5. Calves injected with T. foetus antigen within the first 3 weeks of life, and in which there was evidence of autogenous γ globulin, developed normal autogenous but not induced agglutinins.

6. Calves which received colostrum containing maternal induced and normal agglutinins, calves partially deprived of colostrum, and calves immunized in early life, produced the normal autogenous agglutinin between the 30th and 60th days, reaching the normal adult titre of 1/48–1/96.

7. The properties of the normal agglutinins were investigated. They possess some characteristics significantly different from those of the induced agglutinins. These suggested that the normal agglutinins were γ globulin molecules with an ‘accidental’ genetic configuration complementary to T. foetus.

The author wishes to thank Dr M. Robertson, F.R.S., and Sir Alan Drury, F.R.S. for their interest and encouragement during the course of this work, and Dr R. C. Campbell for the statistical analysis.

Type
Research Article
Information
Journal of Hygiene , Volume 53 , Issue 3 , September 1955 , pp. 261 - 275
Copyright
Copyright © Cambridge University Press 1955

References

Aschapfenburg, R. (1949). Brit. J. Nutr. 3, 200.CrossRefGoogle Scholar
Burnet, F. M. & Fenner, F. (1949). The Production of Antibodies. Australia: Melbourne.Google Scholar
Comline, R. S., Roberts, H. E. & Titchen, D. A. (1951 a). Nature, Lond., 167, 561.CrossRefGoogle Scholar
Comline, R. S., Roberts, H. E. & Titchen, D. A. (1951 b). Nature, Lond., 168, 84.CrossRefGoogle Scholar
Flynn, F. V. & De Mayo, P. (1951). Lancet, ii, 235.CrossRefGoogle Scholar
Gibson, H. J. (1930). J. Hyg., Camb., 30, 337.CrossRefGoogle Scholar
Hanan, R. & Oyama, J. (1954). J. Immunol. 73, 49.CrossRefGoogle Scholar
Hess, E. L. & Deutsch, H. F. (1948). J. Amer. chem. Soc. 70, 84.CrossRefGoogle Scholar
Hess, E. L. & Deutsch, H. F. (1949). J. Amer. chem. Soc. 71, 1376.CrossRefGoogle Scholar
Hess, W. R. (1953 a). Amer. J. vet. Res. 14, 192.Google Scholar
Hess, W. R. (1953 b). Amer. J. vet. Res. 14, 195.Google Scholar
Kekwick, R. A. (1940). Biochem. J. 34, 1248.CrossRefGoogle Scholar
Kekwick, R. A. & Mackay, M. E. (1954). Spec. Rep. Ser. med. Res. Coun, Lond., no. 286.Google Scholar
Kekwick, R. A. & Record, B. R. (1941). Brit. J. exp. Path. 22, 29.Google Scholar
Kerr, W. R. & Robertson, M. (1941). Vet. J. 97, 351.Google Scholar
Kerr, W. R. & Robertson, M. (1943). J. comp. Path. 53, 280.CrossRefGoogle Scholar
Kerr, W. R. & Robertson, M. (1945). Vet. Rec. 57, 221.Google Scholar
Kerr, W. R. & Robertson, M. (1946). J. comp. Path. 56, 38.CrossRefGoogle Scholar
Kerr, W. R. & Robertson, M. (1953). J. Hyg., Camb., 51, 405.CrossRefGoogle Scholar
Kerr, W. R. & Robertson, M. (1954). J. Hyg., Camb., 52, 253.CrossRefGoogle Scholar
Kunkel, H. G. & Tiselius, A. (1952). J. gen. Physiol. 35, 89.CrossRefGoogle Scholar
Loeffler, W. & Wunderly, C. (1953). J. clin. Path. 6, 282.CrossRefGoogle Scholar
Peters, B. A. (1940). Publ. Hlth, Lond., 53, 215.CrossRefGoogle Scholar
Pierce, A. E. (1947). Lab. J. 8, 238.Google Scholar
Pierce, A. E. (1954). Ph.D. Thesis, London University.Google Scholar
Pierce, A. E. (1955). J. Hyg., Camb., 53, 247.CrossRefGoogle Scholar
Zingher, A. (1923). Amer. J. Dis. Child. 25, 392.Google Scholar
Zingher, A. (1924). Amer. J. publ. Hlth, 14, 955.CrossRefGoogle Scholar