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Nutrient Metabolism

Tetrahydrofolates Are Greatly Stabilized by Binding to Bovine Milk Folate-Binding Protein^{1 ,,2}

Department of Biochemistry and Molecular Biology, The University of Queensland, St. Lucia, Queensland 4072, Australia

³To whom correspondence should be addressed. E-mail: p.nixon{at}mailbox.uq.edu.au.

The dietary supply of folates and their measurement are both affected, potentially, by the instability of some folates. Labile folates appear to be stabilized by binding to folate-binding protein (FBP); this paper reports measurements of that stabilization. The degradation rates of the very labile tetrahydrofolate (H₄folate) and moderately labile 5-methyltetrahydrofolate (5-CH₃H₄folate) were measured with the compounds free or bound to either soluble or immobilized bovine milk FBP. Complexation increased stability from 2- to > 1000-fold, depending on buffer and temperature conditions. H₄folate at 4°C and pH 6.7 appeared to be quite stable for > 100 d when bound to soluble FBP but had a half-life of < 1 h when free. Stabilization of milk folates may be a role of FBP and would improve the bioavailability of milk folate to newborns and other consumers.

KEY WORDS: • folate-binding protein • tetrahydrofolate • 5-methyltetrahydrofolate

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