ISOLATION AND PURIFICATION OF RIBOFLAVIN BINDING PROTIEN FROM COOT EGG-YOLK (Fulica atra)
نویسندگان
چکیده
Riboflavin-binding protein (RfBP) was isolated, purified and characterized from Coot (Fulica atra) egg. The RfBP was purified using DEAE-Sepharose ion exchange chromatography followed by gel filtration on Sephadex G-100. The purity of the proteins was judged by SDSPAGE. The protein migrated as a single band on SDS gel with a molecular weight of corresponding to nearly 29 Kd.
منابع مشابه
Isolation, Purification and Characterization of Riboflavin Carrier Protein (RCP) from Emu Egg Yolk (Dromaius novaehollandia)
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 electropho...
متن کاملComparison of Four Different Purification Methods for Isolation of Anti Echis carinatus Antivenom Antibodies from Immunized Chicken Egg Yolk
Egg-laying hens were immunized with the Echis carinatus venom and the resulting antibodies were extracted from egg yolk by four different purification methods. The chicken egg yolk antibodies were purified by the water dilution method, polyethylene glycol (PEG) and ammonium sulphate precipitation method, chloroform extraction and the Lithium sulphate precipitation method. These methods were com...
متن کاملOn hen egg fractionation: applications of liquid chromatography to the isolation and the purification of hen egg white and egg yolk proteins.
Liquid chromatography has been used as a means of egg protein analysis or as a method for the purification of egg proteins. Several chromatographic methods, including gel permeation, ion-exchange, reversed-phase, hydrophobic interaction, and immobilized-ligand-affinity chromatography, have been carried out for the separation or the purification of egg yolk or egg white proteins. Ion-exchange ch...
متن کاملPurification of egg yolk immunoglobulins. A two-step procedure using hydrophobic interaction chromatography and gel filtration.
A two-step chromatographic procedure was developed for the isolation and purification of hen IgY antibodies from egg yolk. The antibodies were completely separated from vitellin and lipids by hydrophobic interaction chromatography followed by gel filtration. Almost no residual yolk proteins, no immunoglobulin aggregates, and no antibody fragments could be detected in the final extract. Moreover...
متن کاملGeneral applicability of chicken egg yolk antibodies: the performance of IgY immunoglobulins raised against the hypoxia-inducible factor 1alpha.
Avian embryos and neonates acquire passive immunity by transferring maternal immunoglobulins from serum to egg yolk. Despite being a convenient source of antibodies, egg yolk immunoglobulins (IgY) from immunized hens have so far received scant attention in research. Here we report the generation and rapid isolation of IgY from the egg yolk of hens immunized against the alpha subunit of the huma...
متن کامل