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Department of Biochemistry, College of Medicine, University of Iowa, Iowa City, Iowa 52240
The production of L-tryptophan and L-kynurenine upon incubating D-tryptophan with liver slices and homogenates from the rabbit and the rat suggested that the kynurenic acid formed from D-tryptophan may have arisen partly through them and partly via D-kynurenine. Kidney slices and homogenates produced L-tryptophan even more readily, but yielded neither D- nor L-kynurenine. The L- and D-isomers of tryptophan and kynurenine were separated and identified by paper chromatography, and assayed quantitatively. Their configurations were confirmed by their reaction with L- or D-amino acid oxidase to yield indolepyruvic acid or kynurenic acid. The production of L-tryptophan from the D-tryptophan occurred in two steps. The first step required oxygen. It yielded indolepyruvic acid under conditions optimal for D-amino acid oxidase activity. The second step involved the conversion of the indolepyruvic acid to L-tryptophan, either in the presence or absence of oxygen, under conditions favoring transamination. Rat tissues effected the overall inversion more readily than rabbit tissues. Differences in the capacities of rat versus rabbit tissue to deaminate the D-tryptophan were more marked than the differences in their capacities to transaminate the indolepyruvic acid. Production of kynurenic acid through oxidative deamination of D-kynurenine and through transamination of L-kynurenine were indicated.
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Manuscript received 22 March 1971.