GLYCOPROTEIN ESTIMATION OF RIBOFLAVIN BINDING PROTEIN (SILVER STAINING) FROM THE EGGS OF COOT (Fulica atra ) AND HEN (Gallus gallus): A COMPARATIVE STUDY

Riboflavin binding protein (RfBP) was isolated from the eggs of Fulica atra and Gallus gallus. The protein was purified in two steps, DEAE- Sepharose ion exchange chromatography followed by gelfilteration on Sephadex G-100. The purity of the protein was judged by SDS-PAGE technique. The Glycoprotein Estimation of Riboflavin binding protein. A single band on the slab and cylindrical gels revealed that the protein was pure. Comparison of the mobility of RfBP with that of the standard molecular weight marker proteins suggested that RfBP from the egg white and yolk of Fulica atra and Hen had a molecular weight close to 29 Kd.