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. Author manuscript; available in PMC: 2025 Aug 27.
Published in final edited form as: Toxicol Sci. 2015 Dec 10;150(1):27–39. doi: 10.1093/toxsci/kfv311

TABLE 2.

Sulfation of Triclosan and Tolvaptan by Individual Human SULTs

SULT pmol.min−1.mg cell lysate protein−1
Triclosana Tolvaptanb

1A1 15.2 ± 1.5 n.d.
1A2 193 ± 4.3 n.d.
1A3 182 ± 9.6 n.d.
1B1 199 ± 9.8 9.0 ± 0.3
1C2 38.6 ± 3.4 n.d.
1C3 22.9 ± 2.8 18.5 ± 0.5
1C4 210 ± 12.8 n.d.
1E1 190 ± 4.0 2.3 ± 0.1
2A1 26.7 ± 4.7 13.8 ± 0.6
2B1 34.1 ± 1.0 2.3 ± 0.2
4A1 20.8 ± 1.6 n.d.
6B1 8.9 ± 0.3 n.d.
a

Sulfation assays were conducted in a 125 μl final reaction volume by incubating 0.25 mM [2,4-dichlorophenyl-14C(U)]triclosan (specific activity: 22.9 mCi/mmol) with 1.2 mg cell lysate proteins, 2 mM EDTA, 0.5 mM PAPS, and 100 mM sodium phosphate, pH 7.2, at 37°C for 2 h. Reactions were terminated by the addition of an equal volume of ice-cold methanol. Precipitated material was removed by centrifugation at 14,000 g at 4°C for 30 min and the supernatants were analyzed for tolvaptan and tolvaptan sulfate by a reversed-phase HPLC with radiochemical detection as previously described (Fang et al., 2014).

b

Sulfation assays using 0.2 mM tolvaptan at 37°C for 1 h, as described in Materials and Methods. n.d.: not detected.