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The 31P nuclear magnetic resonance spectrum of cows' milk

Published online by Cambridge University Press:  01 June 2009

Peter S. Belton ,
Richard L. J. Lyster  and
Colin P. Richards
Peter S. Belton
Affiliation:
Food Research Institute, Norwich NR4 7UA, UK
Richard L. J. Lyster
Affiliation:
† ‡National Institute for Research in Dairying (University of Reading), Shinfield, Reading RG2 9 AT, UK
Colin P. Richards
Affiliation:
§Laboratory of the Government Chemist, London SE1 9NQ, UK
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Summary

The 31P nuclear magnetic resonance spectrum of liquid milk was examined. Of the three peaks observed, the two larger were assigned to inorganic phosphate (Pi) and the seryl phosphate (SerP) residues of casein; the third peak was assigned to a phosphodiester, which is probably glycerophosphoryl choline. The pH-dependences of the chemical shifts of the Pi and SerP were measured with and without added EDTA, and the results confirm the assignments. The width of the Pi peak in milk is significantly greater than in similar solutions lacking casein, probably because of binding to, or chemical exchange with, the casein micelle. Most of the SerP residues in milk are not sufficiently mobile to have been detected in these experiments but a significant fraction of SerP residues is able to move freely and can be titrated.

Type
Original Articles
Information
Journal of Dairy Research , Volume 52 , Issue 1 , February 1985 , pp. 47 - 54
Copyright
Copyright © Proprietors of Journal of Dairy Research 1985

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References

REFERENCES

Belton, P S, Gordon, R E, Jones, J M & Shaw, D 1983 A 31P topical magnetic resonance study of embryonic development in hen's eggs British Poultry Science 24 429–433Google Scholar
Colman, A & Gadian, D G 1976 31P Nuclear magnetic resonance studies on the developing embryos of Xenopus laevis European Journal of Biochemistry 61 387–396Google Scholar
Gadian, D G 1982 Nuclear magnetic resonance and its applications to living systems OxfordOxford University PressGoogle Scholar
Gadian, D G, Radda, G K, Richards, R E & Seeley, P J 1979 31P NMR in living tissue the road from a promising to an important tool in biology In Biological applications of magnetic resonance, pp 463–535, (Ed Shulman, R G) New YorkAcademic PressCrossRefGoogle Scholar
Graham, D E & Phillips, M C 1979 Proteins at liquid interfaces III Molecular structures of adsorbed films Journal of Colloid and Interface Science 70 427–439CrossRefGoogle Scholar
Herzfeld, J, Roufossb, A, Haberkorn, R A, Griffin, R G & Glimcher, M J 1980 Magic angle sample spinning in inhomogeneously broadened biological systems Philosophical Transactions of the Royal Society, London B 289 459–469Google Scholar
Ho, C., Magnuson, J. A., Wilson, J. B., Magnuson, N. S. & Kurland, R. J. 1969 Phosphorus nuclear magnetic resonance studies of phosphoproteins and phosphorylated molecules. II. Chemical nature of phosphorus atoms in αs-casein B and phosvitin. Biochemistry 8 2074–2082CrossRefGoogle Scholar
Humphrey, R. S. & Jolley, K. W. 1982 31P-NMR studies of bovine β-casein. Biochimica et Biophysica Acta 708 294–299Google Scholar
Jacobson, L. & Cohen, J. S. 1981 Improved technique for investigation of cell metabolism by 31P NMR spectroscopy. Bioscience Reports 1 141–150CrossRefGoogle Scholar
Jenness, R. & Koops, J. 1962 Preparation and properties of a salt solution which simulates milk ultrafiltrate. Netherlands Milk and Dairy Journal 16 153–164Google Scholar
Johnson, A. H. 1974 The composition of milk. In Fundamentals of Dairy Chemistry 2nd edn p. 28, (Eds Webb, B. H., Johnson, A. H. and Alford, J. A.) Westport, CT: Avi Publishing Co., Inc.Google Scholar
Lee, S. L., Glonek, T. & Glimoher, M. J. 1983 31P Nuclear magnetic resonance spectroscopic evidence for ternary complex formation of fetal dentin phosphoprotein with calcium and inorganic orthophosphate ions. Calcified Tissue International 35 815–818Google Scholar
Mercier, J. C., Grosclaude, F. & Ribadeau Dumas, B. 1972 Primary structure of bovine caseins. A review. Milchwissenschaft 27 402–408Google Scholar
Ogawa, S., Rottenberg, H., Brown, T. R., Shulman, R. G., Castillo, C. L. & Glynn, P. 1978 Highresolution 31P nuclear magnetic resonance study of rat liver mitochondria. Proceedings of the National Academy of Sciences of the USA 75 1796–1800Google Scholar
Rothwell, W. P., Waugh, J. S. & Yesinowski, J. P. 1980 High-resolution variable-temperature 31P NMR of solid calcium phosphates. Journal of the American Chemical Society 102 2637–2643CrossRefGoogle Scholar
Schmidt, D. G. 1982 Association of caseinsand casein micelle structure. In Developments in Dairy Chemistry - 1 Proteins, pp. 61–86. (Ed. Fox, P. F.) London: Applied Science PublishersGoogle Scholar
Sleigh, R. W., Mackinlay, A. G. & Pope, J. M. 1983 NMR studies of the phosphoserine regions of bovine αsi- and β-casein. Assignment of 31P resonances to specific phosphoserines and cation binding studied by measurement of enhancement of 'H relaxation rate. Biochimica et Biophysica Acta 742 175–183Google Scholar
Slonczewski, J. L., Rosen, B. P., Alger, J. R. & Macnab, R. M. 1981 pH homeostasis in Escherichia coli: measurement by 31P nuclear magnetic resonance of methylphosphonate and phosphate. Proceedings of the National Academy of Science of the USA 78 6271–6275Google Scholar
Tropp, J., Blumenthal, N. C. & Waugh, J. S. 1983 Phosphorus NMR study of solid amorphous calcium phosphate. Journal of the American Chemical Society 105 22–26Google Scholar