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PURIFICATION AND CHARACTERIZATION OF RIBOFLAVIN BINDING PROTEIN FROM THE EGG WHITE OF EAGLE (AQUILA HASTATE)

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Author(s): Madhkar Rao Kudle et al.

Journal: International Journal of Pharmaceutical Sciences and Research
ISSN 0975-8232

Volume: 3;
Issue: 2;
Start page: 494;
Date: 2012;
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Keywords: Aquila hastate | DEAE-Sepharose | Electrophoretic characterization | Riboflavin binding protein (RfBP)

ABSTRACT
Riboflavin binding protein (RfBP) was isolated from the eggs of Aquila hastate (eagle). The protein was purified in two steps, DEAE – Sepharose ion exchange chromatography and gelfilteration on Sephadex G-100. The holoprotein had an absorption spectrum characteristic of flavoproteins. The purity of the protein was judged by SDS-PAGE technique. A single band on the slab and cylindrical gel revealed that the protein was pure comparison of the mobility of RfBP with that of the standard molecular weight marker proteins suggested that RfBP from the egg white of Aquila hastate had a molecular weight close to 29 Kd.
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