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Carbohydrates of bovine κ-casein

Published online by Cambridge University Press:  01 June 2009

J. V. Wheelock  and
G. Sinkinson
J. V. Wheelock
Affiliation:
School of Biological Sciences, The University, Bradford, Yorkshire BD7 1DP
G. Sinkinson
Affiliation:
School of Biological Sciences, The University, Bradford, Yorkshire BD7 1DP
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Summary

Comparison of the carbohydrates of κ-casein with those of the glycopeptides released by the action of rennin on whole milk showed that there are consistent differences between them, which are due to the presence of carbohydrates in para-κ-casein. d-Mannose, d-galactose, 2-acetamido-2-deoxy-d-galactose and N-acetyl neuraminic acid were invariably present in κ-casein. N-acetyl neuraminic acid was located almost entirely on the glycopeptides whereas the greater proportion of d-mannose was attached to the para-κ-casein. d-Galactose and 2-acetamido-2-deoxy-d-galactose were detected in both para-κ-casein and the glycopeptides. In the glycopeptides there are usually about 2 molecules of d-galactose to 1 molecule of 2-acetamido-2-deoxy-d-galactose. Carbohydrates are attached to only a proportion of para-κ-casein molecules. Carbohydrates could not be detected in αs- and β-casein.

Information

Type
Research Article
Information
Journal of Dairy Research , Volume 40 , Issue 3 , October 1973 , pp. 413 - 420
Copyright
Copyright © Proprietors of Journal of Dairy Research 1973

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References

REFERENCES

Alais, C. & Jollès, P. (1961). Biochimica et Biophysica Acta 51, 315.CrossRefGoogle Scholar
Armstrong, C. E., Mackinlay, A. G., Hill, R. J. & Wake, R. G. (1967). Biochimica et Biophysica Acta 140, 123.CrossRefGoogle Scholar
Beeby, R. (1963). Journal of Dairy Research 30, 77.CrossRefGoogle Scholar
Clamp, J. R., Dawson, G. & Hough, L. (1967). Biochimica et Biophysica Acta 148, 342.CrossRefGoogle Scholar
Fiat, A. M., Alais, C. & Jollès, P. (1968). Chimia 22, 137.Google Scholar
Jollès, P., Alais, C. & Jollès, J. (1961). Biochimica et Biophysica Acta 51, 309.CrossRefGoogle Scholar
Mackinlay, A. G. & Wake, R. G. (1965 a). Biochimica et Biophysica Acta 104, 167.CrossRefGoogle Scholar
Mackinlay, A. G. & Wake, R. G. (1965b). Private communication, cited by McKenzie, H. A. (1967), Advances in Protein Chemistry 22, 55.Google Scholar
McCabe, E. M. (1967). Thesis, Michigan State University.Google Scholar
Nitschmann, H., Wissmann, H. & Henzi, R. (1957). Chimia 11, 76.Google Scholar
Sinkinson, G. & Wheelock, J. V. (1970 a). Journal of Dairy Research 37, 113.CrossRefGoogle Scholar
Sinkinson, G. & Wheelock, J. V. (1970 b). Biochimica et Biophysica Acta 215, 517.CrossRefGoogle Scholar
Wake, R. G. (1959). Australian Journal of Biological Sciences 12, 479.CrossRefGoogle Scholar
Waugh, D. F. & von Hippel, P. H. (1956). Journal of the American Chemical Society 78, 4576.CrossRefGoogle Scholar
Yaguchi, M., Davies, D. T. & Kim, Y. K. (1968). Journal of Dairy Science 51, 473.CrossRefGoogle Scholar
Zittle, C. A. & Custer, J. H. (1963). Journal of Dairy Science 46, 1183.CrossRefGoogle Scholar