Human indolylamine 2,3-dioxygenase. Its tissue distribution, and characterization of the placental enzyme
Year: 1985
Type: article
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.
Source: Biochemical Journal
DOI: 10.1042/bj2300635
Authors: F Yamazaki, T Kuroiwa, O Takikawa, R Kido
Institution: Wakayama Medical University
Language: English
Subfield: Biological Psychiatry
Field: Neuroscience
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W1920018418