{"title":"从牛胎盘中分离出一种高比活性的雌激素硫转移酶。","authors":"S S Moore, E O Thompson, A R Nash","doi":"10.1071/bi9880333","DOIUrl":null,"url":null,"abstract":"<p><p>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.</p>","PeriodicalId":8573,"journal":{"name":"Australian journal of biological sciences","volume":"41 3","pages":"333-41"},"PeriodicalIF":0.0000,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"12","resultStr":"{\"title\":\"Oestrogen sulfotransferase: isolation of a high specific activity species from bovine placenta.\",\"authors\":\"S S Moore, E O Thompson, A R Nash\",\"doi\":\"10.1071/bi9880333\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>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.</p>\",\"PeriodicalId\":8573,\"journal\":{\"name\":\"Australian journal of biological sciences\",\"volume\":\"41 3\",\"pages\":\"333-41\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1988-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"12\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Australian journal of biological sciences\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1071/bi9880333\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Australian journal of biological sciences","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1071/bi9880333","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
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.
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