Hostname: page-component-77c89778f8-rkxrd Total loading time: 0 Render date: 2024-07-20T20:19:25.505Z Has data issue: false hasContentIssue false
  • English
  • Français

Human β-casein

Published online by Cambridge University Press:  01 June 2009

Rae Greenberg  and
Merton L. Groves
Rae Greenberg
Affiliation:
Eastern Regional Research Center*, Philadelphia, Pennsylvania 19118, USA
Merton L. Groves
Affiliation:
Eastern Regional Research Center*, Philadelphia, Pennsylvania 19118, USA
Get access Rights & Permissions [Opens in a new window]

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
Information
Journal of Dairy Research , Volume 46 , Issue 2: Symposium on the Physics and Chemistry of Milk Proteins , April 1979 , pp. 235 - 239
Copyright
Copyright © Proprietors of Journal of Dairy Research 1979

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

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