Abstract
Human placental estrogen sulfotransferase (ESFT) was partially purified from the term placental cytosol by (NH 4) 2SO 4 precipitation and agarose gel chromatography. Additional purifications caused a rapid loss of the enzyme activity. The activity was abolished by isoelectrofocusing but partially retained by chromatofocusing. The value of pI of human placental ESFT is 5.8 and the same value was obtained for bovine adrenal ESFT. The enzyme protein was able to bind to the affinity resin, estradiol-17-hemisuccinyl-1,2-diaminododecane sepharose 4B, but difficult to be extracted by estradiol (E 2). The extract of the affinity resin showed one major protein band at 68,000 dalton on SDS-polyacrylamide gel electrophoresis. Kinetic studies using partially purified ESFT revealed that E 2 is the best substrate for this enzyme. The relative rate of sulfurylation of E 2 estrone, estriol and dehydroepi-androsterone at 4 μM ( K m for E 2) is 1, 0.3, 0.08 and 0.08, respectively.
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