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The kinetics of the precipitation of chemically modified αs1-casein by calcium

Published online by Cambridge University Press:  01 June 2009

David S. Horne
David S. Horne
Affiliation:
Hannah Research Institute, Ayr, Scotland, KA6 5HL
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Summary

The aggregation of αs1-casein by Ca is viewed as resulting from a reduction in the net negative charge by the binding of positively charged Ca2+. This reduction in charge leads to the equivalent of isoelectric precipitation. A quantitative relationship between the rate of aggregation of the casein and the monomer net charge is predicted in this isoelectric precipitation model. Precipitation results are presented for αs1-casein labelled with dansyl chloride. Providing the changes in charge brought about by the modification are taken into account, the precipitation behaviour of these caseins can be reconciled with that of native αs1-casein. This emphasises the role of electrostatic repulsion in this process and lends further support to the isoelectric precipitation model.

Type
Section C. Association of Proteins
Information
Journal of Dairy Research , Volume 46 , Issue 2: Symposium on the Physics and Chemistry of Milk Proteins , April 1979 , pp. 265 - 269
Copyright
Copyright © Proprietors of Journal of Dairy Research 1979

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References

REFERENCES

Clarke, R. F. L. & Nakai, S. (1972). Biochimica et Biophysica Acta 257, 70.CrossRefGoogle Scholar
Evans, M. T. A., Irons, L. & Jones, M. (1971). Biochimica et Biophysica Acta 229, 411.CrossRefGoogle Scholar
Hoagland, P. D. (1966). Journal of Dairy Science 49, 783.CrossRefGoogle Scholar
Irons, L., Evans, M. T. A., Jones, M. & Miller, P. J. (1973). Biochimica et Biophysica Acta 328, 133.Google Scholar
Li, E. C. Y. & Nakai, S. (1976). Journal of Food Science 41, 278.Google Scholar
Overbeek, J. Th. G. (1952). In Colloid Science, vol. 1., chap. 7. (Ed. Kruyt, H. R.). Amsterdam: Elsevier.Google Scholar
Parker, T. G. & Dalgleish, D. G. (1977). Biopolymers 16, 2533.CrossRefGoogle Scholar
Pepper, L., Hipp, N. J. & Gordon, W. G. (1970). Biochimica et Biophysica Acta 207, 340.Google Scholar
Rawitch, A. B. & Weber, G. (1972). Journal of Biological Chemistry 247, 680.CrossRefGoogle Scholar
Slattery, C. W. (1976). Journal of Dairy Science 59, 1547.Google Scholar
Woychick, J. H. (1969). Journal of Dairy Science 52, 17.CrossRefGoogle Scholar