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. 2019 Jul 16;14(7):e0219664. doi: 10.1371/journal.pone.0219664

Fig 2. hINMT enzyme activity: 254C vs. 254F.

Fig 2

Comparison of hINMT-catalyzed methylated product formation for 254C (A,C,E) and 254F (B, D, F) (-/+) 15 mM DTT for the substrates tryptamine (A, B), and DMS (C,D). The results for DMSe (E,F) are shown with (+) DTT only. Indicated concentrations of substrates were co-incubated with 5 μg of 254C hINMT or 254F hINMT and 30 μM 14-C S-adenosyl-methionine as described in Materials and Methods. Statistical analysis of results is described in Table 1.