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Human indolylamine 2,3-dioxygenase. Its tissue distribution, and characterization of the placental enzyme
Open accessAbstract
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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Cited by
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Houtkooper, R. H., Cantó, C., Wanders, R. J., & Auwerx, J. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0026 · Cited by 899
Tryptophan metabolism, from nutrition to potential therapeutic applications
Le Floc’h, N., Otten, W., & Merlot, E. (2011) · Amino Acids · doi:10.1007/s00726-010-0752-7 · Cited by 561
Tryptophan degradation in mice initiated by indoleamine 2,3-dioxygenase.
Takikawa, O., Yoshida, R., Kido, R., & Hayaishi, O. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35696-x · Cited by 377
Self-citationMorita, I., Kawamoto, M., & Yoshida, H. (1992) · Journal of Chromatography B: Biomedical Sciences and Applications · doi:10.1016/0378-4347(92)80208-8 · Cited by 47
Metadata
- Authors
- Yamazaki, F., Kuroiwa, T., Takikawa, O., & Kido, R.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- 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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- 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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