抄録
Egg albumin oxidized with iodine reacts with the thiol form of thiamine or O-benzoylthiamine (OBT), forming a protein-thiamine mixed disulfide. The amount of the disulfide formation was markedly decreased by heat or urea denaturation before oxidation. The reactivity was greatest, when the SH-groups of the native protein was oxidized directly. Denaturation after oxidation did not cause any significant change in reactivity. When the SH-groups of the native protein was oxidized after denaturation, the reactivity was lowered with the degree of denaturation. The finding seems to be due to the decreased formation of the intramolecular -S-S-linkages in the protein molecule which are involved in the reaction with the thiol forms of thiamine derivatives owing to the denaturation prior to oxidation.
