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Preparation and properties of β-casein from buffalo's milk

Published online by Cambridge University Press:  01 June 2009

M. H. Abd El-Salam  and
Safinaz El-Shibiny
M. H. Abd El-Salam
Affiliation:
Laboratory of Food Technology and Dairying, National Research Centre, Cairo, Egypt
Safinaz El-Shibiny
Affiliation:
Laboratory of Food Technology and Dairying, National Research Centre, Cairo, Egypt
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Summary

β-Casein from individual buffalo's milk was found to be homogeneous by starch-gel electrophoresis. β-Casein was separated from buffalo's milk by the method of Warner (1944) and purified by DEAE-cellulose chromatography.

Buffalo β-casein possesses identical end-groups to those of cow β-casein; namely N-terminal arginine and assuming a single polypeptide chain a possible C-terminal sequence of Ile-Ile-Val. However, the amino-acid composition and the tryptic peptide patterns of the 2 proteins are not the same.

Type
Research Article
Information
Journal of Dairy Research , Volume 42 , Issue 1 , February 1975 , pp. 163 - 167
Copyright
Copyright © Proprietors of Journal of Dairy Research 1975

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References

REFERENCES

Abd El-Salam, M. H. & El-Shibiny, S. (1972). Journal of Dairy Research 39, 219.CrossRefGoogle Scholar
Annan, W. D. & Manson, W. (1969). Journal of Dairy Research 36, 259.CrossRefGoogle Scholar
Aschaffenburg, R., Sen, A. & Thompson, M. P. (1968). Comparative Biochemistry and Physiology 27, 621.CrossRefGoogle Scholar
Goodwin, T. W. & Morton, R. A. (1946). Biochemical Journal 40, 628.CrossRefGoogle Scholar
Kalan, E. B., Thompson, M. P., Greenberg, R. & Pepper, L. (1965). Journal of Dairy Science 48, 884.CrossRefGoogle Scholar
McKenzie, H. A. (Ed.) (1971). Milk Proteins, vol. 2. New York: Academic Press.Google Scholar
Manson, W. (1961). Archives of Biochemistry and Biophysics 95, 336.CrossRefGoogle Scholar
Moore, S. & Stein, W. H. (1954). Journal of Biological Chemistry 211, 907.CrossRefGoogle Scholar
Nagasawa, T., Kiyosawa, I., Kuwahara, K. & Ganguli, N. C. (1973). Journal of Dairy Science 56, 61.CrossRefGoogle Scholar
Peterson, R. F., Nauman, L. W. & Hamilton, D. F. (1966). Journal of Dairy Science 49, 601.CrossRefGoogle Scholar
Rose, D., Davies, D. T. & Yaguchi, M. (1969). Journal of Dairy Science 52, 8.CrossRefGoogle Scholar
Snell, F. D. & Snell, C. T. (1949). Colorimetric Methods of Analysis, 3rd edn, vol. 2. Princeton, N.J.: D. Van Nostrand & Co.Google Scholar
Spackman, D. H., Stein, W. H. & Moore, S. (1958). Analytical Chemistry 30, 1190.CrossRefGoogle Scholar
Thompson, M. P., Kalan, E. B. & Greenberg, R. (1967). Journal of Dairy Science 50, 767.CrossRefGoogle Scholar
Wake, R. G. & Baldwin, R. L. (1961). Biochimica et Biophysica Acta 47, 225.CrossRefGoogle Scholar
Warner, R. C. (1944). Journal of the American Chemical Society 66, 1725.CrossRefGoogle Scholar