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

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Yamazaki, F, Kuroiwa, T, Takikawa, O, Kido, R·1985·Biochemical Journal

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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Metadata

Authors
Yamazaki, F., Kuroiwa, T., Takikawa, O., & Kido, R.
Venue
Biochemical Journal
Published
1985-09-15
Volume
230
Issue
3
Pages
635-638
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
OpenAlex
W1920018418
Cited by
243
References
0
FWCI
1.47
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Human indolylamine 2,3-dioxygenase. Its tissue distribution, and characterization of the placental enzyme. https://app.cochat.ai/papers/10.1042/bj2300635
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Yamazaki, F., Kuroiwa, T., Takikawa, O., & Kido, R. (1985). Human indolylamine 2,3-dioxygenase. Its tissue distribution, and characterization of the placental enzyme. Biochemical Journal. https://doi.org/10.1042/bj2300635

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.