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Folate binding by human milk protein.

S I Hansen, J Holm, J Lyngbye

    Scandinavian Journal of Clinical and Laboratory Investigation
    |June 1, 1977
    PubMed
    Summary
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    Researchers identified two folate binding protein fractions in human whey. A major fraction exhibits cooperative binding, suggesting a polymerizing protein system involved in folate transport and interaction.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Nutritional Science

    Background:

    • Human whey contains proteins with potential roles in nutrient transport.
    • Folate binding proteins are crucial for folate absorption and metabolism.
    • Understanding protein interactions in whey can reveal insights into nutritional bioavailability.

    Purpose of the Study:

    • To characterize folate binding proteins in human whey.
    • To investigate the binding characteristics and kinetics of these proteins.
    • To explore the potential involvement of protein systems in folate binding.

    Main Methods:

    • Gel chromatography was used to separate protein fractions from human whey.
    • Ion exchange chromatography was employed for isolating specific folate binding proteins.

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  • Equilibrium dialysis and inhibition assays with methotrexate were performed to study binding.

    • Main Results:

    • Two distinct folate binding protein fractions were identified: a major (Mr ~30,000) and a minor (Mr >200,000).
    • The major fraction (FB) demonstrated cooperative binding sites for folate, which were lost upon methotrexate inhibition.
    • Methotrexate competitively inhibited folate binding without altering maximum binding capacity, suggesting a polymerizing protein system.

    Conclusions:

    • Human whey contains a major folate binding protein (FB) with cooperative binding properties.
    • The binding affinity is influenced by FB concentration, indicating a polymerizing system.
    • These findings provide insights into the molecular mechanisms of folate binding and transport in human whey.