Clinical Chemistry
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Clinical Chemistry 26: 1591-1592, 1980;
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Clinical Chemistry, Vol 26, 1591-1592, Copyright © 1980 by American Association for Clinical Chemistry

Cofactor in serum for high-affinity folate binding in milk

J Holm, SI Hansen and J Lyngbye

Affinity-chromatographic purification of the folate-binding protein from whey of cow's milk results in the removal of a heat-resistant cofactor that is important in high-affinity folate binding (Biochim, Biophys. Acta 579: 479, 1979). Thus a shift from negative to positive cooperativity occurred in the presence of cofactor (Biochim, Biophys. Acta 579: 479, 1979). We demonstrate the presence of a similar cofactor in sera from men, pregnant women, and umbilical cords. Even highly diluted (10 000-fold) serum samples were active, and the cofactor was also present in erythrocyte hemolysates (10 000-fold diluted). The identity of the cofactor, which may act as an overall modulator of high- affinity folate binding, is still obscure.




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Copyright © 1980 by the American Association for Clinical Chemistry.