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Isolation and characterization of thiamin-binding protein from chicken egg white

Muniyappa, K and Adiga, PR (1979) Isolation and characterization of thiamin-binding protein from chicken egg white. In: Biochemical Journal, 177 (3). pp. 887-894.

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A thiamin-binding protein was isolated and characterized from chicken egg white by affinity chromatography on thiamin pyrophosphate coupled to aminoethyl-Sepharose. The high specificity of interaction between the thiamin-binding protein and the riboflavin-binding protein of the egg white, with a protein/protein molar ratio of 1.0, led to the development of an alternative procedure that used the riboflavin-binding protein immobilized on CNBr-activated Sepharose as the affinity matrix. The thiamin-binding protein thus isolated was homogeneous by the criteria of polyacrylamide-gel disc electrophoresis, double immunodiffusion and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, had a mol.wt. of 38,000 +/- 2000 and was not a glycoprotein. The protein bound [14C]thiamin was a molar ratio of 1.0, with dissociation constant (Kd) 0.3 micrometer.

Item Type: Journal Article
Publication: Biochemical Journal
Publisher: Portland Press
Additional Information: Copyright of this article belongs to Portland Press.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 23 Dec 2010 07:45
Last Modified: 01 Mar 2012 06:40
URI: http://eprints.iisc.ac.in/id/eprint/34361

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