Hostname: page-component-7bb8b95d7b-dtkg6 Total loading time: 0 Render date: 2024-09-16T12:14:11.619Z Has data issue: false hasContentIssue false
  • English
  • Français

Serological studies on heat-induced interactions of α-lactalbumin and milk proteins

Published online by Cambridge University Press:  01 June 2009

A. Baer ,
M. Oroz  and
B. Blanc
A. Baer
Affiliation:
Federal Dairy Research Institute, CH-3097 Liebefeld-Bern, Switzerland
M. Oroz
Affiliation:
Federal Dairy Research Institute, CH-3097 Liebefeld-Bern, Switzerland
B. Blanc
Affiliation:
Federal Dairy Research Institute, CH-3097 Liebefeld-Bern, Switzerland
Get access Rights & Permissions [Opens in a new window]

Summary

The heat denaturation of α-lactalbumin (α-la) in NaCl and KCl solutions, milk ultrafiltrate and milk was studied using the method of micro complement fixation. It was established that this protein was very resistant to heat denaturation and that it was more stable in milk ultrafiltrate than in the other media studied at temperatures up to 70 °C. Of the various milk proteins added to α-la, only β-lactoglobulin (β-lg) formed a heat-induced complex with this protein. This complex was identical in milk ultrafiltrate or in milk and depended on the molar ratio between both proteins; it was not modified by any other milk proteins. The binding of a-la to β-lg changed the ability of the latter protein to bind κ-casein.

Type
Original Articles
Information
Journal of Dairy Research , Volume 43 , Issue 3 , October 1976 , pp. 419 - 432
Copyright
Copyright © Proprietors of Journal of Dairy Research 1976

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

Armstrong, J. McD., Hopper, K. E., McKenzie, H. A. & Murphy, W. H. (1970). Biochemica et Biophysica Acta 214, 419.CrossRefGoogle Scholar
Brew, K., Vanaman, T. C. & Hill, R. L. (1967). Journal of Biological Chemistry 242, 3747.CrossRefGoogle Scholar
Dupont, M. (1965). Biochimica et Biophysica Acta 102, 500.CrossRefGoogle Scholar
Gordon, W.G.(1971). In Milk Proteins, vol. 2, p. 347. (Ed. McKenzie, H. A..) New York: Academic Press.Google Scholar
Gordon, W. G. & Ziegler, J. (1955). Archives of Biochemistry and Biophysics, 57, 80.Google Scholar
Hunter, W. M. (1967). In Handbook of Experimental Immunology, p. 608. (Ed. Weir, D. M..) Oxford: Blackwell Scientific Publications.Google Scholar
Hunziker, H. G. & Tarassuk, N. P. (1965). Journal of Dairy Science 48, 733.CrossRefGoogle Scholar
Kronman, J. M. & Andreotti, R. E. (1964). Biochemistry 3, 1145.CrossRefGoogle Scholar
Levine, L. (1967). In Handbook of Experimental Immunology, p. 707. (Ed. Weir, D. M..) Oxford: Black well Scientific Publications.Google Scholar
Levine, L. & Van Vunakis, H. (1967). Methods in Enzymology 11, 928.CrossRefGoogle Scholar
Lyster, R. L. J. (1970). Journal of Dairy Research 37, 233.CrossRefGoogle Scholar
McKenzie, H. A. & Wake, R. G. (1961). Biochimica et Biophysica Acta 47, 240.CrossRefGoogle Scholar
Ouchterlony, O. (1967). In Handbook of Experimental Immunology, p. 655. (Ed. Weir, D. M..) Oxford: Blackwell Scientific Publications.Google Scholar
Rüegg, M., Lüscher, M. & Blanc, B. (1974). Journal of Dairy Science 57, 387.CrossRefGoogle Scholar
Sawyer, W. H. (1969). Journal of Dairy Science 52, 1347.CrossRefGoogle Scholar
Takesada, H., Nakanishi, M. & Tsuboi, M. (1973). Journal of Molecular Biology 77, 605.CrossRefGoogle Scholar
Visser, J., Deonier, R. C., Adams, E. T. Jr & Williams, J. W. (1973). Biochemistry 11, 2634.CrossRefGoogle Scholar
Zittle, C. A., Thompson, M. P., Custer, J. H. & Cerbulis, J. (1962). Journal of Dairy Science 45, 807.CrossRefGoogle Scholar