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<b>PURIFICATION AND PROPERTIES OF ESTROGEN SULEOTRANSFERASE OF HUMAN FETAL </b><b>LIVER </b>

DOIFull Paper Access

10

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0

References

1993

Year

TAKAAKI HONDOH, Takashi Suzuki, KUMIKO HIRATO, Hiroshi Saitoh, Tsuyoki Kadofuku, Tsuneo Sato, T Yanaihara
Biomedical Research

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 ,uM and 35.6 nmol/mg protein/min, respectively. Although cytosol sulfotransferase activity for pregnenolone is 6.8-fold higher than that for estrone when pregnenolone is incubated with the purified enzyme, sulfotransferase activity for pregnenolone diminishes to about one-twentieth of that for estrone.