Purification and properties of riboflavin-binding protein from the egg white of the duck (Anas platyrhynckos).

Muniyappa, K and Adiga, Radhakantha P (1980) Purification and properties of riboflavin-binding protein from the egg white of the duck (Anas platyrhynckos). In: Biochimica et Biophysica Acta (BBA) - Protein Structure, 623 (2). pp. 339-347.

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Abstract

Riboflavin-binding protein was purified from the egg white of domestic duck and some of its properties were investigated. The protein was homogeneous by the criteria of gel filtration on Sephadex G-100 and electrophoresis on sodium dodecyl sulphate-polyacrylamide gels, had molecular weight of 36 000 ± 1000 and, unlike the chicken egg white protein (Mr 32 000 ± 2000), was devoid of covalently-bound carbohydrate. It was similar to the chicken riboflavin-binding protein in its behavior on ion-exchange celluloses and affinity to interact with the flavin and its coenzymes, but differed significantly in amino acid composition in that it completely lacked proline and contained less of methionine and arginine. The protein partially cross-reacted with the specific antiserum to chicken riboflavin-binding protein with a spur during immunodiffusion analysis.

Item Type:	Journal Article
Publication:	Biochimica et Biophysica Acta (BBA) - Protein Structure
Publisher:	Elsevier Science
Additional Information:	Copyright of this article belongs to Elsevier Science.
Keywords:	Riboflavin-binding protein; Molecular weight estimation; Amino acid composition; (Anas platyrhynckos)
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	05 Nov 2009 09:11
Last Modified:	29 Feb 2012 09:38
URI:	http://eprints.iisc.ac.in/id/eprint/21729

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