PMID: 109083Mar 1, 1979

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

The Biochemical Journal
K Muniyappa, P R Adiga


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.


Mar 1, 1983·Experimental Neurology·J E Bergquist, M Hanson
Jan 1, 1985·Annals of the New York Academy of Sciences·H B White
Aug 28, 2007·Proteomics·Karlheinz Mann

Related Concepts

Carrier Proteins
Chromatography, Affinity
Egg White Proteins
Egg Whites
Immunodiffusion Measurement
Thiamine Mononitrate

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