A riboflavin carrier protein has been purified from human pregnancy and umbilical cord sera by affinity chromatography and fast protein liquid chromatography. This protein has a similar molecular weight to the chicken egg riboflavin carrier protein and shares other physicochemical properties, such as pI and riboflavin binding characteristics, with the avian counterpart. A high degree of immunological cross-reactivity is observed between the human and avian riboflavin binding proteins indicating the extensive conservation of this protein throughout evolution.

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