Dephosphorylation of sodium caseinate, enzymatically hydrolyzed casein and casein phosphopeptides by intestinal alkaline phosphatase: implications for iron availability

Author:

Yeung Andrew C.,Glahn Raymond P.,Miller Dennis D.

Publisher

Elsevier BV

Subject

Clinical Biochemistry,Nutrition and Dietetics,Molecular Biology,Biochemistry,Endocrinology, Diabetes and Metabolism

Reference27 articles.

1. Gaucheron, F., Graet, L.E., Boyaval, Y. and Piot, E, Binding of cations to sodium caseinate: importance of physicochemical conditions, Milchwissen, 52, 322–327 (1997).

2. Pabon, M.L., & Lonnerdal B, Distribution of iron and its bioavailability from iron-fortified milk and formula, Nutr Res, 12, 975–984 (1992).

3. Hurrell, R. F., Lynch, S. R., Trinidad, T. P., Dassenko, S. A. & Cook, J. D, Iron absorption in humans as influenced by bovine milk proteins, Am J Clin Nutr, 49, 546–552 (1989).

4. Emery, T, Iron oxidation by casein, Biochem Biophys Res Comm, 182, 1047–1052 (1992).

5. Bernos, E., Girardet, J.M., Humbert, G., & Linden G, Role of the O-phosphoserine clusters in the interaction of the bovine milk αs1-, β-, κ-caseins and the PP3 component with immobilized iron (III) ions, Biochim Biophys Acta, 1337, 149–159 (1997).

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