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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Sulfation of minoxidil by human platelet sulfotransferase.

In an attempt to determine whether (1) sulfotransferase activity in human platelets would convert minoxidil to minoxidil sulfate and (2) inter-subject variations in this sulfotransferase activity could be noted, platelet homogenates were incubated with minoxidil and 35S-PAPS in HEPES buffer at 37 degrees C for 30 min. Radioactivity which was extracted into ethyl acetate and shown by HPLC to elute with authentic minoxidil sulfate was counted by scintillation counting. Aliquots of the platelet homogenates were also preincubated at 43 degrees C for 15 min to determine the thermal stability of the sulfotransferase activity. Sulfotransferase activity in platelets from 48 adult males ranged from 0.9-13.2 pmol minoxidil sulfate produced/10(7) platelets per 30 min (mean 4.91 +/- 2.84 pmol/10(7) platelets per 30 min +/- SD). Thermal stable sulfotransferase activity ranged from 0.2-7.6 pmol minoxidil produced/10(7) platelets per 30 min and varied from 15 to 57% of the total sulfotransferase activity. Thus, the results indicate that human platelets can effect the sulfation of minoxidil and that sulfotransferase activity does show inter-subject variation.[1]

References

  1. Sulfation of minoxidil by human platelet sulfotransferase. Johnson, G.A., Baker, C.A. Clin. Chim. Acta (1987) [Pubmed]
 
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