Isolation, Purification and Characterization of Riboflavin Carrier Protein (RCP) from Emu Egg Yolk (Dromaius novaehollandia)
نویسندگان
چکیده
Riboflavin carrier (or binding) protein (RCP) was isolated from the Emu egg yolk (Dromaius novaehollandia) for the first time. In the present study an attempt has been made to isolate and purify the RCP in two steps, DEAE Sephadex A-50 ion exchange chromatography and the final purification was achieved on sephadex G-100.The purity of the protein was judged on cylindrical and slab gel electrophoresis,SDS-PAGE technique. Sephadex G100 re-chromatographic fraction RCP moved as a single band both on the slab and cylindrical gels. Comparison of the mobility of the RCP isolated from Emu egg yolk with that of the standards molecular weight marker proteins revealed that the molecular weight of the protein is higher than 29 kDa.
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