The folate in cow's milk was strongly and specifically bound to a minor whey protein (FP), forming a complex of primary M of about 38000, but exhibiting concentration-dependent reversible aggregation. The binding protein was present in excess, and the milk had the capacity to bind about 50 μg added folic acid/l. An enriched concentrate of FP was prepared by ammonium sulphate fractionation—FP was precipitated at between 50 and 60% saturation—and further purified by chromatography in DEAE-cellulose and filtration in Sephadex gel G150. Its identity as a distinct minor whey protein was confirmed by comparative starch gel electrophoresis at various pH values. Some properties of the protein are described, and its physiological significance discussed. © 1969, Proprietors of Journal of Dairy Research. All rights reserved.