[Preparation of thiamine derivative-protein complexes].
The formation of a thiamine -- egg albumin complex through the action of thiamine propylidsulphide on native, heat denatured and iodine oxidized albumin was studied. The reaction was carried out at pH 6 to 10, temperature 20 degrees to 45 degrees C, and with varying proportions of substrates in the reaction mixture. The content of thiamine in thiamine propyldisulphide and the amount of protein -- bound thiamine were measured by the thiochromic method after the vitamin containing substance had been reduced with sodium thiosulphate or cysteine. It was found that thiamine was complexed with protein due to the reaction between thiamine propyldisulphide and oxidized albumin, pH optimum being 9. The chemical equilibrium shifted towards the complex with excessive protein used. The reaction between thiamine propyldisulphide and sulphdryl groups of proteins yielded a protein--S-propylic radical complex, pH optimum being 7.3. Calculations of kinetic parameters of the process indicated that it was endothermic.
D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008722:Methods; D010047:Ovalbumin; D011485:Protein Binding; D013696:Temperature; D013831:Thiamine / Q000031:analogs & derivatives*
D010047:Ovalbumin; C013294:prosultiamine; D013831:Thiamine
Poluchenie kompleksov proizovodnykh tiamina s belkom.