Hostname: page-component-78c5997874-ndw9j Total loading time: 0 Render date: 2024-11-14T04:27:56.890Z Has data issue: false hasContentIssue false
  • English
  • Français

Electrophoretic and Immunological Studies on Sera from Calves from Birth to Weaning I. Electrophoretic Studies

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 serum proteins of calves from birth to weaning, and the maternal colostral whey have been examined with the ‘classical’ Tiselius electrophoresis apparatus. Differences were shown between calves fed colostrum and those partially deprived of colostrum.

2. A study of the pre-colostral calf serum showed the presence of albumin and of two major components with mobilities similar to the α and β globulins of adult serum. A component forming approximately 1·4 % of the total serum proteins and with a mobility similar to that of γ1 or fibrinogen represented the γ1 globulin. This globulin component was not unconverted fibrinogen and may be autogenous γ globulin or γ globulin passively acquired in utero.

3. Autogenous γ globulin was evident in colostrum-fed and colostrum-deprived calves shortly after birth. The γ1 and γ2 components could be distinguished by the 10th day after birth, at which time the γ1 globulin was the greater. By the 30th day the γ2 globulin exceeded the γ1 globulin and a smaller component termed the γ3 globulin could usually be detected between the γ2 and the salt boundary.

4. Albumin concentrations generally fluctuated inversely to changes in the total serum globulins.

5. The α globulins associated with fetuin declined shortly after birth in the colostrum-fed group. In the deprived group α globulin first rose and then fell. In both groups minimum α globulin values were reached at about the 30th day, when the α1 globulin, although initially the major component in pre-colostral calf serum, was more depleted than the α2.

6. The β globulin frequently showed a transient though marked increase when the α globulins were at their lowest values.

7. No changes in the electrophoretic mobilities of the major serum proteins were detected as the calves matured, and no significant difference was found between the mobilities of the electrophoretic components of calf and adult sera.

8. The electrophoretic examination of colostral whey, colostral lacto-globulin fractions and calf serum immediately after suckling usually showed one lacto-globulin component. The relationship between the serum γ globulins and the lacto-globulin. is discussed.

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, Dr W. R. Kerr for his co-operation in supplying most of the serum and colostrum samples, and Dr A. W. Stableforth and Dr J. S. Paterson for making certain cattle available for these experiments.

Type
Research Article
Information
Journal of Hygiene , Volume 53 , Issue 3 , September 1955 , pp. 247 - 260
Copyright
Copyright © Cambridge University Press 1955

References

Bradish, C. J. & Brooksby, J. B. (1954). Biochem. J. 56, 342.CrossRefGoogle Scholar
Bradish, C. J., Henderson, W. M. & Brooksby, J. B. (1954 a). Biochem. J. 56, 329.CrossRefGoogle Scholar
Bradish, C. J., Henderson, W. M. & Brooksby, J. B. (1954 b). Biochem. J. 56, 335.CrossRefGoogle Scholar
Deutsch, H. F. (1954). J. biol. Chem. 208, 669.CrossRefGoogle Scholar
Deutsch, H. F. & Goodloe, M. B. (1945). J. biol. Chem. 161, 1.CrossRefGoogle Scholar
Hansen, R. G. & Phillips, P. H. (1947). J. biol. Chem. 171, 223.CrossRefGoogle Scholar
Hogness, K. R., Giffee, J. W. & Koenig, V. L. (1946). Arch. Biochem. 10, 281.Google Scholar
Howe, P. E. (1921). J. biol. Chem. 49, 115.CrossRefGoogle Scholar
Howe, P. E. (1924). J. exp. Med. 39, 313.CrossRefGoogle Scholar
Jameson, E., Alvarez-Tostado, C. & Sortor, H. H. (1942). Proc. Soc. exp. Biol. N.Y., 51, 163.CrossRefGoogle Scholar
Janssen, L. W. (1951). Verh. Akad. Wet. Amst. 47, 36.Google Scholar
Little, R. B. & Orcutt, M. L. (1922). J. exp. Med. 35, 161.CrossRefGoogle Scholar
Longsworth, L. G. (1942). Chem. Rev. 30, 323.CrossRefGoogle Scholar
Mason, J. H., Dalling, T. & Gordon, W. S. (1930). J. Path. Bact. 33, 783.CrossRefGoogle Scholar
Miller, L. L. & Bale, W. F. (1954). J. exp. Med. 99, 125.CrossRefGoogle Scholar
Miller, L. L., Bly, C. G. & Bale, W. F. (1954). J. exp. Med. 99, 133.CrossRefGoogle Scholar
Murray, M., Johnson, S. A. & Seegers, W. H. (1954). Science, 119, 293.CrossRefGoogle Scholar
Pedersen, K. O. (1944). Nature, Lond., 154, 575.CrossRefGoogle Scholar
Pedersen, K. O. (1945). Ultracentrifugal Studies on Serum and Serum Fractions. Upsala.Google Scholar
Pedersen, K. O. (1947). J. phys. Chem. 51, 164.CrossRefGoogle Scholar
Philpot, J. St L. (1938). Nature, Lond., 141, 283.CrossRefGoogle Scholar
Pierce, A. E. (1955). J. Hyg., Camb., 53, 261.CrossRefGoogle Scholar
Polson, A. (1952). Onderstepoort J. vet. Sci. 25, 7.Google Scholar
San Clemente, C. L. & Huddleson, I. F. (1943). Tech. Bull. Mich, agric. Exp. Sta., no. 182.Google Scholar
Scatchard, G., Batchelder, A. C. & Brown, A. (1946). J. Amer. chem. Soc. 68, 2320.CrossRefGoogle Scholar
Smith, E. L. (1946 a). J. biol. Chem. 164, 345.CrossRefGoogle Scholar
Smith, E. L. (1946 b). J. biol. Chem. 165, 665.CrossRefGoogle Scholar
Smith, T. & Little, R. B. (1922). J. exp. Med. 36, 181.CrossRefGoogle Scholar
Smith, T. & Little, R. B. (1924). J. exp. Med. 39, 303.CrossRefGoogle Scholar
Svensson, H. (1946). Ark. Kemi. Min. Geol. 22A, 156.Google Scholar
Tiselius, A. (1937). Trans. Faraday Soc. 33, 524.CrossRefGoogle Scholar
Tiselius, A. & Kabat, E. A. (1939). J. exp. Med. 69, 119.CrossRefGoogle Scholar
Wehmeyer, P. (1949). Rev. Immunol. 13, 57.Google Scholar