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

ABSTRACT

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.