Abstract
Minoxidil sulphotransferase (MST) activity was determined in the cytosolic fraction of rat skin and liver. MST of rat skin is similar to the P (phenol)-form of phenolsulphotransferase (PST) of human tissues with respect to thermostability and inhibition by 2,6-dichloro-4-nitrophenol (DCNP). p-Nitrophenol, a prototype substrate of human P-PST form, inhibits MST at micromolar concentration while millimolar concentrations of dopamine and tyramine, substrates of human M-(monoamine)-PST, are required to elicit a similar degree of inhibition. The enzymatic transfer of 35S from sodium 35sulphate to minoxidil was also demonstrated suggesting that the rat skin is potentially capable of synthesizing 3'-phosphoadenosine-5'-phosphosulphate (PAPS) from inorganic sulphate and utilizing it for the biosynthesis of minoxidil sulphate, its active metabolite. Thus, it is conceivable that the pharmacological action of minoxidil as a promotor of hair growth could be carried out by the cutaneous tissues without the contribution of hepatic or other extrahepatic organs.
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