Characterization of Recombinant Human Liver Thermolabile Phenol Sulfotransferase with Minoxidil as the Substrate

P. E. Kudlacek, D. L. Clemens, Robert J. Anderson

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Minoxidil, a potent antihypertensive agent and hair growth stimulator, is metabolized by phenol sulfotransferase to its activated form, minoxidil sulfate. The thermostable form of phenol sulfotransferase was reported to be the enzyme that catalyzed the reaction. Our previous findings with partially purified human platelet preparations indicated that the thermolabile form of phenol sulfotransferase also catalyzed the sulfation of minoxidil. To confirm and to characterize precisely the activity of thermolabile phenol sulfotransferase toward minoxidil, we investigated the ability of the enzyme expressed from a human liver cDNA clone to sulfate minoxidil during testing of thermal stability and of inhibition by 2,6-dichloro-4-nitrophenol and NaCl. The cDNA encoded thermolabile phenol sulfotransferase activity assayed with minoxidil behaved in the same fashion as the activity measured with dopamine, a finding that confirmed that this enzyme activity sulfated minoxidil. Thus, thermolabile phenol sulfotransferase must be taken into account with the thermostable enzyme when estimating the human tissue sulfotransferase contribution to minoxidil sulfation.

Original languageEnglish
Pages (from-to)363-369
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume210
Issue number2
DOIs
StatePublished - May 16 1995
Externally publishedYes

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Arylsulfotransferase
Minoxidil
Liver
Substrates
Enzymes
Complementary DNA
Sulfotransferases
Enzyme activity
Platelets
Hair
Antihypertensive Agents
Dopamine
Thermodynamic stability
Blood Platelets
Clone Cells
Hot Temperature
Tissue
Testing
Growth

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology
  • Biophysics
  • Biochemistry

Cite this

Characterization of Recombinant Human Liver Thermolabile Phenol Sulfotransferase with Minoxidil as the Substrate. / Kudlacek, P. E.; Clemens, D. L.; Anderson, Robert J.

In: Biochemical and Biophysical Research Communications, Vol. 210, No. 2, 16.05.1995, p. 363-369.

Research output: Contribution to journalArticle

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AB - Minoxidil, a potent antihypertensive agent and hair growth stimulator, is metabolized by phenol sulfotransferase to its activated form, minoxidil sulfate. The thermostable form of phenol sulfotransferase was reported to be the enzyme that catalyzed the reaction. Our previous findings with partially purified human platelet preparations indicated that the thermolabile form of phenol sulfotransferase also catalyzed the sulfation of minoxidil. To confirm and to characterize precisely the activity of thermolabile phenol sulfotransferase toward minoxidil, we investigated the ability of the enzyme expressed from a human liver cDNA clone to sulfate minoxidil during testing of thermal stability and of inhibition by 2,6-dichloro-4-nitrophenol and NaCl. The cDNA encoded thermolabile phenol sulfotransferase activity assayed with minoxidil behaved in the same fashion as the activity measured with dopamine, a finding that confirmed that this enzyme activity sulfated minoxidil. Thus, thermolabile phenol sulfotransferase must be taken into account with the thermostable enzyme when estimating the human tissue sulfotransferase contribution to minoxidil sulfation.

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