Tetrahydrofolates Are Greatly Stabilized by Binding to Bovine Milk Folate-Binding Protein

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 t...

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Bibliographic Details
Published inThe Journal of nutrition Vol. 132; no. 9; pp. 2690 - 2694
Main Authors Jones, Martina L., Nixon, Peter F.
Format Journal Article
LanguageEnglish
Published Bethesda, MD Elsevier Inc 01.09.2002
American Society for Nutritional Sciences
American Institute of Nutrition
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Summary: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.
Bibliography:http://jn.nutrition.org/content/132/9.toc
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ISSN:0022-3166
1541-6100
DOI:10.1093/jn/132.9.2690