Oestrogen sulfotransferase: isolation of a high specific activity species from bovine placenta.
During the course of a study of the control of expression of steroid-binding proteins in human mammary cancer oestrogen sulfotransferase was isolated from bovine placenta. By a combination of salt precipitation and ion-exchange and gel-permeation chromatography two forms of the enzyme were isolated. The forms, which apparently differ only in charge, have specific activities 100-300 times greater than has previously been reported for the enzyme. Partial peptide sequences of these enzymes are presented.
Moore
S S
SS
Oncology Research Centre, Prince of Wales Hospital, Randwick, N.S.W.
Thompson
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EO
Nash
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AR
D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004789:Enzyme Activation; D005260:Female; D006801:Humans; D010920:Placenta / Q000201:enzymology*; D013045:Species Specificity; D015238:Sulfotransferases; D013466:Sulfurtransferases / Q000096:biosynthesis / Q000302:isolation & purification*
D013466:Sulfurtransferases; D015238:Sulfotransferases; C020122:estrone sulfotransferase