Isolation and characterization of riboflavin-binding protein from pregnant-rat serum

Muniyappa, K and Adiga, PR (1980) Isolation and characterization of riboflavin-binding protein from pregnant-rat serum. In: Biochemical Journal, 187 (2). pp. 537-540.

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Abstract

A high-affinity riboflavin -binding protein was isolated and characterized for the first time from pregnant-rat sera by affinity chromatography on a lumiflavin-agarose column. The purified protein was homogeneous by the criteria of analytical polyacrylamide-gel disc electrophoresis, gel-filtration chromatography on Sephadex G-100 and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. It had a molecular weight of 90000+/-5000 and interacted with [14C]riboflavin with a 1:1 molar ratio with a dissociation constant (Kd) of 0.42 micron.

Item Type:	Journal Article
Publication:	Biochemical Journal
Publisher:	The Biochemical Society
Additional Information:	Copyright of this article belongs to the Biochemical Society.
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	27 Aug 2009 05:25
Last Modified:	01 Mar 2012 06:38
URI:	http://eprints.iisc.ac.in/id/eprint/22389

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