Studies on high-performance liquid chromatography with electrochemical detection. The pH-dependency of enzymic sulfation of catechol estrogens.
- 1 January 1985
- journal article
- research article
- Published by Pharmaceutical Society of Japan in CHEMICAL & PHARMACEUTICAL BULLETIN
- Vol. 33 (2) , 685-689
- https://doi.org/10.1248/cpb.33.685
Abstract
In vitro sulfation of catechol estrogens with guinea pig and rat liver homogenates was investigated by means of high-performance liquid chromatography with electrochemical detection. When incubated in a neutral medium (pH 7.4) with the liver 105,000 g supernatant fortified with 3''-phosphoadenosine-5''-phosphosulfate, 2-hydroxyestrone and 4-hydroxyestrone were transformed principally into the 2- and 4-sulfates, respectively. The 3-sulfate was formed, and decreasing amounts of the 2- and 4-sulfates were obtained, as the pH of the incubation medium was decreased. The pH effect on directive glucuronidation was also examined with catechol estrogens. The product ratio of the isomeric ring A glucuronides formed was not affected by the pH of the incubation medium.This publication has 7 references indexed in Scilit:
- In vitro metabolic conjugation of catechol estrogensJournal of Steroid Biochemistry, 1984
- Partial purification and characterization of two isoenzymes involved in the sulfurylation of catecholaminesBiochemical and Biophysical Research Communications, 1982
- Multiple forms of phenolsulphotransferase in human tissuesBiochemical Pharmacology, 1982
- On the mechanism of aryl sulfotransferase.Journal of Biological Chemistry, 1981
- Enzymatic sulfation of steroidsAnalytical Biochemistry, 1979
- The effect of hydrogen ion concentration on enzymatic O-methylation of catechol estrogens. Clinical analysis on steroids. XI.Journal of Pharmacobio-Dynamics, 1979
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951