Riboflavin binding protein (RfBP) is one of the several nutrient-binding proteins with primary function of depositing riboflavin in the egg. Riboflavin binding protein was isolated and purified from Ostrich (Struthio camelus) egg white and yolk by DEAE Sepharose ion exchange chromatography followed by gel filtration chromatography on Sephadex G-100. The purity of the protein was judged by SDS-PAGE technique. Comparison of the mobility of the purified proteins with the standard molecular weight marker proteins revealed that the Ostrich RfBP (egg white and yolk) had a molecular weight close to 54 kDa and it was approximately 25 kDa larger than the hen egg white RfBP.
