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A Docile Method of Isolation and Purification of Riboflavin Binding Protein (Rfbp) from Peahen (Pavo cristatus) and Domestic Fowl (Gallus gallus)


Affiliations
1 Dept of Zoology, & Dept of Bio- chemistry, Kakatiya University, Warangal-506009, India
 

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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  • A Docile Method of Isolation and Purification of Riboflavin Binding Protein (Rfbp) from Peahen (Pavo cristatus) and Domestic Fowl (Gallus gallus)

Abstract Views: 903  |  PDF Views: 117

Authors

G. Rajender
Dept of Zoology, & Dept of Bio- chemistry, Kakatiya University, Warangal-506009, India
G. Benarjee
Dept of Zoology, & Dept of Bio- chemistry, Kakatiya University, Warangal-506009, India
M. S. K. Prasad
Dept of Zoology, & Dept of Bio- chemistry, Kakatiya University, Warangal-506009, India
B. Laxma Reddy
Dept of Zoology, & Dept of Bio- chemistry, Kakatiya University, Warangal-506009, India
B. Narayana Rao
Dept of Zoology, & Dept of Bio- chemistry, Kakatiya University, Warangal-506009, India

Abstract


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

References





DOI: https://doi.org/10.17485/ijst%2F2009%2Fv2i11%2F29532