Abstract
Estrogen sulfotransferase was purified approximately 1,800-fold from human fetal liver cytosol and the properties of this enzyme were investigated. The major steps in the purification procedure included DEAE-Sepharose CL-6B chromatography, column chromatofocusing and adenosine 3',5'-diphosphate-agarose affinity chromatography. The purified estrogen sulfotransferase has a molecular mass of approximately 36 kDa on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The purified estrogen sulfotransferase is active toward estrone; the apparent Km and Vmax values are 1.66 μM and 35.6 nmol/mg protein/min, respectively
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