Abstract
Thiamine-protein complex is formed by the reaction of O-benzoyl thiamine disulfide or other symmetrical thiamine disulfides with proteins such as heat-denatured egg albumin. The complex is not separated into the components by means of solvent extraction or zone electrophoresis, but thiamine is liberated through reduction by sodium thiosulfate. This complex formation does not occur when the denatured protein is treated with iodine or monoiodoacetic acid, showing evidently the participation of protein-SH. The complex formation seems to be produced by the interchange reaction between protein-SH and disulfide type thiamine.
