- Piperazine estrone sulfate preparation method
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The invention relates to a high-purity estra-1,3,5(10)-triene-17-one-3-piperazine sulfate (1:1) (i.e., piperazine estrone sulfate) preparation method, which has characteristics of mild reaction conditions, simple post-treatment operation and easy impurity control, so that the quality of the prepared piperazine estrone sulfate is controllable, and the stability is high. The preparation method comprises the following main steps: 1) dissolving estrone in an organic solvent, and carrying a reaction with a sulfonating reagent to obtain estra-1,3,5(10)-triene-17-one-3-sulfate; and 2) dissolving piperazine in an organic solvent, then adding into the organic solution of the estra-1,3,5(10)-triene-17-one-3-sulfate, separating out a solid, filtering, washing, and drying to obtain the high-purity piperazine estrone sulfate product.
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Paragraph 0027-0029; 0033-0035; 0039-0041
(2020/01/03)
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- Testosterone sulfotransferase: Evidence in the guinea pig that this reaction is carried out by 3α-hydroxysteroid sulfotransferase
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During the course of isolating, characterizing, and cloning estrogen and 3-hydroxysteroid sulfotransferases from the guinea pig adrenal gland, it was noted that cytosolic preparations from this tissue would also sulfonate testosterone. Therefore, we set out to isolate and clone the enzyme that performs this reaction. Testosterone sulfotransferase (TST) was isolated from the guinea pig adrenal by using the standard procedures of ion exchange, affinity, and high-performance liquid chromatography. When purified, TST was examined by liquid-phase nondenaturing isoelectric focusing, it was found that the TST activity profile completely overlapped with the activity profile of the 3α-hydroxysteroid sulfotransferase (3αHST) isoform, but not the 3β-hydroxysteroid sulfotransferase (3βHST) isoform. This finding was further investigated by overexpressing the cDNAs for 3αHST and 3βHST in Escherichia coli and examining the expressed proteins for TST activity. This experiment confirmed that 3αHST does indeed function as a TST. In addition, 3αHST was also found to sulfonate estradiol but not estrone, a finding that further suggested that 3αHST may function as a general 17β-hydroxysteroid sulfotransferase. Copyright (C) 1999.
- Park, Byoung C.,Lee, Young C.,Strott, Charles A.
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p. 510 - 517
(2007/10/03)
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