抄録
It was reported by Esselen and Fuller that a certain strain of E.coli has the activity of reducing dehydroascorbic acid. Authors first observed dehydroascorbic acid reductase in E.coli K_<12>. The enzyme was effective on hydrogen donors such as glutathione, homocysteine, thioglycolate and cysteine, but not effective on reduced NAD, reduced NADP, CoA and lipoic acid. Recently, authors observed that as long as pyruvate exists in the medium containing E.coli, dehydroascorbic acid is reduced. As this reducing activity is independent of dehydroascorbic acid reductase, a new pathway has been suspected. As this reducing activity is dependent upon a pyruvate oxidase system, dehydroascorbic acid is assumed to be reduced into ascorbic acid following reaction sequences in the bacterial cells. The same reactions were found in pig heart muscle.
