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

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

Martina L Jones, Peter F Nixon

J Nutr. 2002 Sep;132(9):2690-4.

PMID: 12221230

Abstract:

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 (H(4)folate) and moderately labile 5-methyltetrahydrofolate (5-CH(3)H(4)folate) 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. H(4)folate at 4 degrees 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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42412120	Folate binding protein from bovine milk			Price

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