Hostname: page-component-848d4c4894-m9kch Total loading time: 0 Render date: 2024-06-05T11:50:41.216Z Has data issue: false hasContentIssue false
  • English
  • Français

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
Get access Rights & Permissions [Opens in a new window]

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

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

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