Purification and characterization of riboflavin binding protein (RfBp) from hen (Gallus gallus) eggs using deae-sepharose column chromatography.

Riboflavin binding protein (RfBP) was isolated, purified and characterized from Hen (Gallus gallus) egg white and yolk using Sepharose column chromatography. The Rfbp was purified using DEAE-Sepharose ion exchange chromatography followed by gel filtration on Sephadex G-100. The protein content was estimated with Lowry method. The purity of the proteins was judged by SDS-PAGE technique. The protein migrated as a single band on SDS gel with a molecular weight of 29 kilodaltons. This is the first report on purification of this protein using DEAE-Sepharose column chromatography.