Purification and Characterization of Rat Liver Minoxidil Sulphotransferase

September 1990 in “ Biochemical Journal ”

Sharon J. Hirshey, Charles N. Falany

minoxidil minoxidil sulphotransferase Mx-ST sulphation rat liver cytosol sulphotransferases phenols PNP Rogaine

Studysummary This study reports the purification of a specific sulphotransferase from rat liver that catalyzes the sulphation of minoxidil, potentially implicating it in minoxidil's bioactivation.

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The paper describes the purification and characterization of rat liver minoxidil sulphotransferase (Mx-ST), an enzyme responsible for the sulphation of minoxidil in rat liver cytosol. The enzyme was purified using various chromatography procedures and was found to exist as a homodimer with a subunit molecular mass of approximately 35,000 Da. Mx-ST is related to a family of STs that are capable of sulphating small phenols such as PNP. The study provides information on the purification and characterization of Mx-ST in rat liver tissue.

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Human platelets change minoxidil to minoxidil sulfate, helping blood vessels widen.

research Biochemical Mechanisms by Which Minoxidil Sulfate Influences Mammalian Cells

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This study observed that the active metabolite minoxidil sulfate promotes vascular relaxation by enhancing potassium permeability, which may inform understanding of minoxidil's antihypertensive and hair growth effects.

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