Abstract
The complex fomation of protein with thiamine or its derivatives was found to be much influenced with the pH values, and, at neutral ranges, thiamine and dibenzoylthiamine were almost entirely adsorbed on protein and thiamine propyldisulfide was adsorbed about 30%, while, at the extreme acidity (pH 1.0), these three compounds and also pyrimidine and thiazole moieties of thiamine were not adsorbed. At neutral, protein could adsorb not only thiamine but also the components of this, and, at relatively higher concentrations, thiazole moiety was more adsorbed on protein than pyrimidine, while, at lower concentrations, this was in reverse.
