Abstract

Comparison of riboflavin binding protein (Rfbp) purified and isolated from egg-yolk, egg-white of Peacock (Pavo cristatus)

Author(s): G.Rajender, G.Benarjee, M.S.K.Prasad

Riboflavin binding protein (RfBP) was isolated from the peacock (Pavo cristatus) egg-yolk, Egg-white. Rfbp was purified on DEAE-SephadexA- 50 followed by Sephadex G-100 ion exchange chromatography. The holoprotein with the bound riboflavin showed an absorption maximum at 455nm.The high intensity of colored peak fraction protein content was estimated.The purity of the protein was judged by cylindrical and slab - gels, SDS-PAGE technique. This protein showed a single band on SDS gels. RfBP of Peacock egg-yolk, egg-white also migrated as a single band during electrophoresis pattern on SDS-PAGE. Comparison of the mobilities of the molecular weightmakers with the mobility of peacock egg-yolk RfBP suggested that the RfBP had a molecular weight of approximately 29,000 kD.Interestingly purified peacock egg-yolk RfBP and purified peacock egg-white RfBP had approximately the same molecular weight as revealed by their electrophoresismobilities on SDS-PAGE.