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. 2014 Jan 9;4:3618. doi: 10.1038/srep03618

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(A) Initial rate of activity of the purified catalytic domain of human TPH2 (v) was assayed in the presence of 0 (), 2 () or 10 () mM QN at different concentrations of the L-tryptophan substrate [S]. Points are means from three replicate determinations of v. SEMs were smaller than the dimensions of the symbols. The data are presented as substrate saturation curves (left panel) and Lineweaver-Burk plots (right). (B) As in (A) but where [S] refers to different concentrations of the TPH2 co-factor 6MePH₄.

Inline graphic — (A) Initial rate of activity of the purified catalytic domain of human TPH2 (v) was assayed in the presence of 0 (), 2 () or 10 () mM QN at different concentrations of the L-tryptophan substrate [S]. Points are means from three replicate determinations of v. SEMs were smaller than the dimensions of the symbols. The data are presented as substrate saturation curves (left panel) and Lineweaver-Burk plots (right). (B) As in (A) but where [S] refers to different concentrations of the TPH2 co-factor 6MePH₄.