Isolation and purifecation of riboflavin binding protein from eagle egg-yolk (aquila hastate).

Riboflavin binding protein was purified from the egg yolk of Aquila hastate (Eagle). The protein was purified using DEAE Sepharose ion exchange chromatography followed by gel filtration on Sephadex G-100. The purity of the protein was judged by cylindrical and slab SDSPAGE techniques. Comparison of the mobility of RfBP with that of the standard molecular weight marker protein revealed that the RfBP had a molecular weight close to 29 Kd. Interestingly the RfBPs from hen egg yolk and eagle egg yolk had the same molecular weights as revealed by the SDS PAGE.