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.
Research Article| March 01 1979
Isolation and characterization of thiamin-binding protein from chicken egg white
Biochem J (1979) 177 (3): 887–894.
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K Muniyappa, P R Adiga; Isolation and characterization of thiamin-binding protein from chicken egg white. Biochem J 1 March 1979; 177 (3): 887–894. doi: https://doi.org/10.1042/bj1770887
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