Abstract
Sarcoplasmic proteins including their soluble enzymes were interacted with B_1・HC1 and various kinds of thiamine derivatives, such as O-benzoylthiamine disulfide (BTDS), O-isobutylthiamine disulfide (IBuTDS), thiamine disulfide (TDS), and thiamine pyrophosphate (TPP) at 37℃ for 1 hour. After dialysis of reaction mixtures, protein-bound complexes were isolated by means of the starch gel electrophoresis, and combined thiamine was determined by the analysis of free thiamine after the treatment using Takadiastase or sodium thiosulfate. Results indicated that BTDS was reacted with albumin, while IBuTDS was especially reacted with lactate dehydrogenase protein in rat muscle. In the case of rabbit muscle, TDS and IBuTDS were shown to have an unknown pattern of combined thiamine in the cathode side on the starch gel electrophoresis. TPP showed many patterns seemed to be probably with peptides in the reaction with the rat and rabbit muscle.
