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Human β-casein

Published online by Cambridge University Press:  01 June 2009

Rae Greenberg
Affiliation:
Eastern Regional Research Center*, Philadelphia, Pennsylvania 19118, USA
Merton L. Groves
Affiliation:
Eastern Regional Research Center*, Philadelphia, Pennsylvania 19118, USA

Summary

Human β-casein occurs in multiphosphorylated forms having the same amino acid composition but with 0–5 phosphate groups/molecule. Sequence analysis was used to determine whether each of the phosphorylated forms is a mixture of species having a certain number of phosphate groups randomly distributed or whether each form contains phosphate groups on specific seryl or threonyl residues. It was found that forms containing 2, 4 and 5 phosphate groups/molecule are homogeneous with respect to their phosphorylation sites. The monophosphorylated form, however, is a mixture of equal amounts of species phosphorylated at residues 9 or 10.

Type
Section B. Milk Proteins: Comparative Aspects, and the Study of some of the Minor Caseins
Copyright
Copyright © Proprietors of Journal of Dairy Research 1979

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References

REFERENCES

Addeo, F., Mercies, J. -C. & Ribadeau Dumas, B. (1977). Journal of Dairy Research 44, 455.Google Scholar
Brignon, G., Ribadeau Dumas, B., Mercier, J. -C., Pelissier, J. P. & Das, B. C. (1977). FEBS Letters 76, 274.CrossRefGoogle Scholar
Goldberqer, R. F. (1967). Methods in Enzymology 11, 317.CrossRefGoogle Scholar
Greenberg, R., Groves, M. L. & Peterson, R. F. (1976). Journal of Dairy Science 59, 1016.Google Scholar
Groves, M. L. & Gordon, W. G. (1970). Archives of Biochemistry and Biophysics 140, 47.Google Scholar
Groves, M. L. & Greenberg, R. (1978). Biochemical Journal 169, 337.Google Scholar
Mckenzie, R. M. & Larson, B. L. (1978). Journal of Dairy Science 61, 723.CrossRefGoogle Scholar
Mercier, J. -C., Grosolaude, F. & Ribadeau Dumas, B. (1971). European Journal of Biochemistry 23, 41.Google Scholar
Nagasawa, T., Kiyosawa, I. & Kuwahara, K. (1970). Journal of Dairy Science 53, 136.Google Scholar
Tsuda, T. (1976). Nippon Shonika Gakkai Zasshi 80, 397.Google Scholar
Voguno, G. F., Caone, M. & Ponzone, A. (1975). Biomedicine 23, 343.Google Scholar
Whitney, R., Brtjnner, J. R., Ebner, K. E., Farrell, H. M., Josephson, R. V., Morr, C. V. & Swaisgood, H. E. (1976). Journal of Dairy Science 59, 795.Google Scholar