文章基本信息

标题：Isolation and Characterization of an Alicyclic Amine N-Sulfotransferase from Female Rat Liver
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作者：Youichi NARITOMI ; Toshiro NIWA ; Toshifumi SHIRAGA 等
期刊名称：Biological and Pharmaceutical Bulletin
印刷版ISSN：0918-6158
电子版ISSN：1347-5215
出版年度：1994
卷号：17
期号：8
页码：1008-1011
DOI：10.1248/bpb.17.1008
出版社：The Pharmaceutical Society of Japan
摘要：An alicyclic amine N-sulfotransferase sulfonating 4-phenyl-1, 2, 3, 6-tetrahydropyridine (PTHP) was purified from female rat liver cytosol and showed a homogeneous band with a molecular weight of 30500 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme, designated NST-1, catalyzed sulfonation not only of the alicyclic amine but also dehydroepiandrosterone, a typical substrate of hydroxysteroid sulfotransferases (STs), but had little sulfonating activity towards 2-naphthol, a typical substrate of aryl STs. The N-terminal amino acid sequence for the first 24 residues had a high homology with those of rat liver hydroxysteroid STs. Therefore, it is suggested that NST-1 is classified as a member of the hydroxysteroid ST. Immunoblot analysis of male and female rat liver cytosol, carried out by using rabbit antisera raised against NST-1, indicated that the female cytosol contained a higher level of the enzyme than that of male. The marked sex difference in the expression level of NST-1 was in good accordance with the previous demonstration that female rat liver cytosol catalyzed sulfonation of PTHP to a greater extent than that of male.
关键词：rat liver cytosol;sulfotransferase;alicyclic amine;dehydroepiandrosterone