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Cofactor in serum for high-affinity folate binding in milk

J Holm, S I Hansen, J Lyngbye

    Clinical Chemistry
    |October 1, 1980
    PubMed
    Summary

    A heat-resistant cofactor crucial for high-affinity folate binding was identified in cow's milk whey. This cofactor, also found in human sera and red blood cells, modulates folate binding cooperativity.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Nutritional Science

    Background:

    • High-affinity folate binding is essential for cellular processes.
    • A heat-resistant cofactor influencing folate binding was previously observed in cow's milk whey.
    • The precise role and identity of this cofactor remain largely unknown.

    Purpose of the Study:

    • To investigate the presence and activity of a heat-resistant cofactor in human biological samples.
    • To determine if this cofactor modulates folate binding affinity and cooperativity in humans.
    • To explore the potential physiological significance of this cofactor in folate metabolism.

    Main Methods:

    • Affinity-chromatographic purification of folate-binding protein from cow's milk whey.
    • Assays to detect cofactor activity in human serum and erythrocyte hemolysates.
    • Analysis of folate binding cooperativity in the presence and absence of the cofactor.

    Main Results:

    • Purification of folate-binding protein removed a heat-resistant cofactor essential for high-affinity binding.
    • The cofactor induced a shift from negative to positive cooperativity in folate binding.
    • A similar active cofactor was detected in human serum (men, pregnant women, umbilical cord) and diluted erythrocyte hemolysates.

    Conclusions:

    • A heat-resistant cofactor modulating high-affinity folate binding is present in human biological fluids and cells.
    • This cofactor plays a significant role in the regulation of folate binding.
    • Further research is needed to elucidate the identity and precise function of this important cofactor.

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