作者: F Yamazaki , T Kuroiwa , O Takikawa , R Kido
DOI: 10.1042/BJ2300635
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摘要: The presence of indolylamine 2,3-dioxygenase was examined in human subjects by determining its activity with L-tryptophan as substrate. Enzyme detected various tissues, and relatively high the lung, small intestine placenta. Human 2,3-dioxygenase, partially purified from placenta, had an Mr about 40 000 gel filtration exhibited a single pI 6.9. enzyme required reducing system, ascorbic acid Methylene Blue, for maximal able to oxidize D-tryptophan, 5-hydroxy-L-tryptophan well L-tryptophan, but kinetic studies indicated that best substrate L-tryptophan.