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. 1985 Sep 15;230(3):635–638. doi: 10.1042/bj2300635

Human indolylamine 2,3-dioxygenase. Its tissue distribution, and characterization of the placental enzyme.

F Yamazaki, T Kuroiwa, O Takikawa, R Kido
PMCID: PMC1152665  PMID: 3877502

Abstract

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

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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