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 language | English |
|---|---|
| Pages (from-to) | 363-369 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 210 |
| Issue number | 2 |
| DOIs | |
| State | Published - May 16 1995 |
| Externally published | Yes |
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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 journal › Article
}
TY - JOUR
T1 - Characterization of Recombinant Human Liver Thermolabile Phenol Sulfotransferase with Minoxidil as the Substrate
AU - Kudlacek, P. E.
AU - Clemens, D. L.
AU - Anderson, Robert J.
PY - 1995/5/16
Y1 - 1995/5/16
N2 - 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.
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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UR - http://www.scopus.com/inward/citedby.url?scp=0029027552&partnerID=8YFLogxK
U2 - 10.1006/bbrc.1995.1670
DO - 10.1006/bbrc.1995.1670
M3 - Article
C2 - 7755612
AN - SCOPUS:0029027552
VL - 210
SP - 363
EP - 369
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -