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Human indolylamine 2,3-dioxygenase. Its tissue distribution, and characterization of the placental enzyme by F Yamazaki; T Kuroiwa; O Takikawa; R Kido is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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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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Author

F Yamazaki; T Kuroiwa; O Takikawa; R Kido

Published

1985

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)