Indian Journal of Science and Technology
Year: 2009, Volume: 2, Issue: 11, Pages: 32-34
G. Rajender, G. Benarjee, M.S.K. Prasad, B. Laxma Reddy and B. Narayana Rao
Dept of Zoology, & Dept of Bio- chemistry, Kakatiya University, Warangal-506009, India.
*Author for the correspondence:
Dept of Zoology, & Dept of Bio- chemistry, Kakatiya University,
E-mail: [email protected]
Riboflavin binding protein (Rfbp) was isolated from domestic fowl (Gallus gallus) and peahen (Pavo cristatus) egg-white and egg-yolk. The protein was purified in two steps, DEAE-Sephadex A-50 ion exchange chromatography and eluted with phosphate buffer pH 7.3 containing 0.5 M sodium chloride. The final purification of protein was achieved on Sephadex G-100. The purity of the protein was judged on cylindrical and slab gel electrophoresis, SDS-PAGE technique. Sephadex G-100 fraction Rfbp moved as a single band both on the Slab and Cylindrical gels. Comparison of the mobility of Rfbp with that of the standard molecular weight marker proteins revealed with that the Rfbp had a molecular weight close to 29,000 kd. Interestingly, hen egg-white Rfbp and peahen egg- white, yolk Rfbp had the same molecular weight as revealed by the SDS-PAGE. This is a novel approach for the study of riboflavin binding protein purified from different avian eggs in two steps and studied electrophoretic characterization with standard molecular weight marker.
Keywords: Rfbp purification method, peahen, hen, egg white-yolk, SDS, PAGE/Native
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