Abstract
Thiamine liberation from thiamine 8-(methyl 6-acetyldihydrothioctate) disulfide (TATD) in erythrocyte hemolysate, which contained glucose-6-phosphate dehydrogenase coupled glutathione reductase (GSSG-reductase) system, was accelerated by addition of NADPH or NADP plus glucose-6-phosphate. On the other hand this acceleration effect was not observed in dialyzed hemolysate. However the acceleration effect was reappeared by addition of limited amount of reduced glutathione (GSH) to dialyzed hemolysate. Acceleration effect by NADPH under the presence of catalytic amount of GSH was also observed on thiamine liberation from thiamine propyldisulfide and thiamine disulfide in dialyzed hemolysate. Activities of GSSG-reductase system were found in dialyzed and non-dialyzed hemolysate in reasonable amount for these acceleration effects. Addition of TATD stimulated ^<14>CO_2 production from glucose-1-^<14>C and -2-^<14>C by wased erythrocytes suspension. These results show a occurrence of the coupling mechanism between GSH oxidation by thiamine disulfide derivatives and glucose-6-phosphate dehydrogenase coupled GSSG reductase system in erythrocytes.
