PURIFICATION AND CHARACTERIZATION OF RIBOFLAVIN BINDING PROTEIN FROM THE EGG WHITE OF EAGLE (AQUILA HASTATE)
AbstractRiboflavin 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.
Article Information
27
494-496
539KB
1102
English
IJPSR
Madhkar Rao Kudle*, Satheesh Kumar Boddu and Prasad MSK
Department of Biochemistry, Kakatiya University, Warangal- 506 009, West Bengal, India
30 September, 2011
10 November, 2011
29 January, 2012
http://dx.doi.org/10.13040/IJPSR.0975-8232.3(2).494-96
1-February-2012
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