Change in binding properties of folate-binding protein in cow's whey due to removal of a cofactor during affinity chromatographic purification.
The folate-binding protein in cow's whey was purified by affinity chromatography on folate or methotrexate-AH-Sepharose 4B. A change in basic binding properties of the protein occurred probably due to the fact that material removed during affinity chromatography contains a cofactor of great importance to folate binding.
D000818:Animals; D001665:Binding Sites; D002352:Carrier Proteins / Q000032:analysis* / Q000378:metabolism; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D002846:Chromatography, Affinity; D005492:Folic Acid / Q000378:metabolism*; D008892:Milk / Q000032:analysis*; D011485:Protein Binding
D002352:Carrier Proteins; D005492:Folic Acid