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Heat-induced interaction of β-lactoglobulin and κ-casein

Published online by Cambridge University Press:  01 June 2009

G. H. McKenzie ,
R. S. Norton  and
W. H. Sawyer
G. H. McKenzie
Affiliation:
Russell Grimwade School of Biochemistry, University of Melbourne, Parkville, Victoria 3052, Australia
R. S. Norton
Affiliation:
Russell Grimwade School of Biochemistry, University of Melbourne, Parkville, Victoria 3052, Australia
W. H. Sawyer
Affiliation:
Russell Grimwade School of Biochemistry, University of Melbourne, Parkville, Victoria 3052, Australia
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Summary

The interaction of β-lactoglobulin and κ-casein at high temperature was studied polarimetrically. The rate of interaction was related to the genetic variant of β-lactoglobulin present. β-Lactoglobulin B, whose thermodenaturation was faster than that of A variant, interacted more rapidly with κ-casein than did the A variant. Velocity sedimentation studies indicated that characteristics of the complex were determined more by the β-lactoglobulin than by the κ-casein. The presence of κ-casein during the thermodenaturation of β-lactoglobulin appeared to prevent the aggregation of β-lactoglobulin from proceeding to completion, the κ-casein complexing with intermediate species and restricting the aggregation process.

Type
Original Articles
Information
Journal of Dairy Research , Volume 38 , Issue 3 , October 1971 , pp. 343 - 351
Copyright
Copyright © Proprietors of Journal of Dairy Research 1971

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References

REFERENCES

Armstrong, J. MCD., Mckenzie, H. A. & Sawyer, W. H. (1967). Biochim. biophys. Acta 147, 60.CrossRefGoogle Scholar
Guggenheim, E. A. (1926). Phil. Mag. 2, 538.CrossRefGoogle Scholar
Kannan, A. & Jenness, R. (1961). J. Dairy Sci. 44, 808.CrossRefGoogle Scholar
Kawahara, K., Kirshner, A. G. & Tanford, C. (1965). Biochemistry 4, 1203.CrossRefGoogle Scholar
Mckenzie, H. A. (1967). Adv. Protein Chem. 22, 56.Google Scholar
Mckenzie, H. A. & Sawyer, W. H. (1967). Nature, Lond. 214, 1101.CrossRefGoogle Scholar
Mckenzie, H. A., Sawyer, W. H. & Smith, M. B. (1967). Biochim. biophys. Acta 147, 73.CrossRefGoogle Scholar
Purkayastha, R., Tessier, H. & Rose, D. (1967). J. Dairy Sci. 50, 764.CrossRefGoogle Scholar
Sawyer, W. H. (1966). Thesis, Australian National University.Google Scholar
Sawyer, W. H. (1969). J. Dairy Sci. 52, 1347.CrossRefGoogle Scholar
Sawyer, W. H., Coulter, S. T. & Jenness, R. (1963). J. Dairy Sci. 46, 564.CrossRefGoogle Scholar
Sawyer, W. H., Norton, R. S., Nichol, L. W. & Mckenzie, G. H. (1971). Biochim. biophys. Acta 243, 19.CrossRefGoogle Scholar
Tessier, H., Yaguchi, M. & Rose, D. (1969). J. Dairy Sci. 52, 139.CrossRefGoogle Scholar
Trautman, J. C. & Swanson, A. M. (1958). J. Dairy Sci. 41, 715.Google Scholar
Zittle, C. A. & Custer, J. H. (1963). J. Dairy Sci. 46, 1183.CrossRefGoogle Scholar
Zittle, C. A., Thompson, M. P., Custer, J. H. & Cerbulis, J. (1962). J. Dairy Sci. 45, 807.CrossRefGoogle Scholar