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A procedure for the partial fractionation of the αs-casein complex

Published online by Cambridge University Press:  01 June 2009

P. F. Fox  and
J. Guiney
P. F. Fox
Affiliation:
Department of Dairy and Food Chemistry, University College, Cork, Irish Republic
J. Guiney
Affiliation:
Department of Dairy and Food Chemistry, University College, Cork, Irish Republic
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Summary

A method for the partial fractionation of the αs-casein complex is described. It involves removal of κ-casein from iso-electric casein by the method of Zittle & Custer (1963) followed by fractionating the residue (αs- and β-casein) by the urea procedure of Hipp et al. (1952). αs0- and αs1-caseins precipitate from 3·3 M urea at pH 4·6, but much of the αs2-, αs3- and αs4-casein remains in solution and co-precipitates with β-casein from 1·7 M urea at pH 4·9. Chromatography on DEAE cellulose clearly separates β-casein from the αs2-, αs3- and αs4-caseins, which are not resolved by the conditions employed. The method is suitable for the fractionation of iso-electric casein into all its major components (i) κ-casein; (ii) αs0- and αs1-caseins; (iii) αs2-, αs3- and αs4-caseins; (iv) β-casein; (v) γ-casein.

Type
Research Article
Information
Journal of Dairy Research , Volume 39 , Issue 1 , February 1972 , pp. 49 - 53
Copyright
Copyright © Proprietors of Journal of Dairy Research 1972

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References

REFERENCES

Annan, W. D. & Manson, W. (1969). J. Dairy Res. 36, 259.CrossRefGoogle Scholar
El-Negoumy, A. M. (1967). Biochim. biophys. Acta 140, 503.CrossRefGoogle Scholar
Hipp, N. J., Groves, M. L., Custer, J. H. & McMeekin, T. L. (1952). J. Dairy Sci. 35, 272.CrossRefGoogle Scholar
Hoagland, P. D., Peterson, R. F., Thompson, M. P. & Kalan, E. B. (1971). J. Dairy Sci. 54, 766.Google Scholar
Rose, D., Brunner, J. R., Kalan, E. B., Larson, B. L., Melnychyn, P., Swaisgood, H. E. & Waugh, D. F. (1970). J. Dairy Sci. 53, 1.CrossRefGoogle Scholar
Thompson, M. P. & Kiddy, C. A. (1964). J. Dairy Sci. 47, 626.CrossRefGoogle Scholar
Thompson, M. P., Kiddy, C. A., Johnston, J. O. & Weinberg, R. M. (1964). J. Dairy Sci. 47, 378.CrossRefGoogle Scholar
Thompson, M. P., Tarassuk, N. P., Jenness, R., Lillevik, H. A., Ashworth, U. S. & Rose, D. (1965). J. Dairy Sci. 48, 159.CrossRefGoogle Scholar
Wake, R. G. & Baldwin, R. L. (1961). Biochim. biophys. Acta 47, 225.CrossRefGoogle Scholar
Zittle, C. A. & Custer, J. H. (1963). J. Dairy Sci. 46, 1183.CrossRefGoogle Scholar