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The reaction of αs1- and β-casein with ferrous ions in the presence of oxygen

Published online by Cambridge University Press:  01 June 2009

W. Manson  and
J. Cannon
W. Manson
Affiliation:
The Hannah Research Institute, Ayr, Scotland, KA6 5HL
J. Cannon
Affiliation:
The Hannah Research Institute, Ayr, Scotland, KA6 5HL
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Summary

The reaction of αs1- and β-casein with ferrous ions and O2 has been studied. It has been found that phosphoseryl residues present in these proteins rapidly catalyse the oxidation of iron from the ferrous to the ferric state with the formation of stable ferric-phosphoprotein complexes and the consumption of the theoretical amount of O2. When, however, the phosphoseryl residues occurred in groups, the formation of ferric complexes was accompanied by uptakes of O2 in quantities significantly in excess of that required for the oxidation of ferrous to ferric iron.

The significance of these findings is discussed in relation to hypotheses which have been advanced concerning the possible biological function of phosphoprotein.

Information

Type
Original Articles
Information
Journal of Dairy Research , Volume 45 , Issue 1 , February 1978 , pp. 59 - 67
Copyright
Copyright © Proprietors of Journal of Dairy Research 1978

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References

REFERENCES

Allen, R. J. L. (1940). Biochemical Journal 34, 858.Google Scholar
Anfinsen, C. B. & Haber, E. (1961). Journal of Biological Chemistry 236, 1361.CrossRefGoogle Scholar
Donella, A., Pinna, L. A. & Moret, V. (1972). FEBS Letters 26, 249.Google Scholar
Grant, C. T. & Taborsky, G. (1966). Biochemistry 5, 544.Google Scholar
Manson, W. (1967 a). Archives of Biochemistry and Biophysics 122, 370.CrossRefGoogle Scholar
Manson, W. (1967 b). Proceedings of the Nutrition Society 26, xvii.Google Scholar
Manson, W. & Annan, W. D. (1971). Archives of Biochemisty and Biophysics 145, 16.Google Scholar
Manson, W. & Carolan, T. (1972). Journal of Dairy Research 39, 189.Google Scholar
Mellander, O. & Vahlqvist, B. (1957). American Journal of Clinical Nutrition 5, 493.Google Scholar
österberg, R. (1959). Arkiv för Kemi 13, 393.Google Scholar
Pape, L., Multani, J. S., Stitt, C. & Saitman, P. (1968). Biochemistry 7, 613.CrossRefGoogle Scholar
Rosenstein, R. W. & Taborsky, G. (1970). Biochemistry 9, 649.Google Scholar
Sandell, E. B. (1950). Colorimetric Determination of Traces of Metals, p. 362. New York, N.Y.: Inter science.Google Scholar
Spackman, D. H., Stein, W. H. & Moore, S. (1958). Analytical Chemistry 30, 1190.CrossRefGoogle Scholar
Taborsky, G. (1963). Biochemistry 2, 266.Google Scholar
Umbreit, W. W., Burris, R. H. & Stauffer, J. F. (1964). Manometric Techniques, 4th edn.Minneapolis, Minn.: Burgess.Google Scholar