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Biochimica et biophysica acta (2017-08-08)
Takuyu Hashiguchi, Katsuhisa Kurogi, Takehiko Shimohira, Takamasa Teramoto, Ming-Cheh Liu, Masahito Suiko, Yoichi Sakakibara
RESUMEN

Cytosolic sulfotransferase (SULT)-mediated sulfation is generally known to involve the transfer of a sulfonate group from the active sulfate, 3'-phosphoadenosine 5'-phosphosulfate (PAPS), to a hydroxyl group or an amino group of a substrate compound. We report here that human SULT2A1, in addition to being able to sulfate dehydroepiandrosterone (DHEA) and other hydroxysteroids, could also catalyze the sulfation of Δ

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Sigma-Aldrich
Aldosterone, ≥95% (HPLC)
Sigma-Aldrich
trans-Dehydroandrosterone, ≥99%
Sigma-Aldrich
1,4-Androstadiene-3,17-dione