1998 Volume 44 Issue 2 Pages 323-328
A thiamin-binding protein from buckwheat (Fagopyrum esculentum Moench) seeds gave two bands of 56- and 50-kDa in the absence of 2-mercaptoethanol and a single band of 25-kDa in the presence of 2-mercaptoethanol on sodium dodecylsulfate gel electrophoresis. These results indicate that the protein consists of polypeptides linked by disulfide bond(s). The protein isolated from buckwheat seeds did not have immunological homology with the thiamin-binding proteins from rice seeds and sesame seeds. However, the binding of the protein to thiamin was inhibited by the modification of the carboxyl residues in the protein as well as that of the thiamin-binding protein from rice seeds. These results suggest that the thiamin-binding protein from buckwheat seeds differs from those from rice seeds and sesame seeds as to subunit structure or immunological properties, but resembles them in the mechanism of binding thiamin.
