{"title":"亲和层析法纯化谷氨酸棒状杆菌中预苯酸脱水酶。","authors":"S Bertaux, R G Harrison","doi":"10.1080/10826069108018578","DOIUrl":null,"url":null,"abstract":"<p><p>Prephenate dehydratase has been purified from the wild type strain Corynebacterium glutamicum by affinity chromatography. Three ligands, L-Trp, L-Tyr, and L-Phe have been tested as well as conditions for elution. L-Phe is the most specific ligand: it leads to a purification factor of 11 in one step using step gradients of NaCl in Tris-HCl buffer at pH 7.5.</p>","PeriodicalId":20391,"journal":{"name":"Preparative biochemistry","volume":"21 4","pages":"269-75"},"PeriodicalIF":0.0000,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10826069108018578","citationCount":"3","resultStr":"{\"title\":\"Purification of prephenate dehydratase from Corynebacterium glutamicum by affinity chromatography.\",\"authors\":\"S Bertaux, R G Harrison\",\"doi\":\"10.1080/10826069108018578\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Prephenate dehydratase has been purified from the wild type strain Corynebacterium glutamicum by affinity chromatography. Three ligands, L-Trp, L-Tyr, and L-Phe have been tested as well as conditions for elution. L-Phe is the most specific ligand: it leads to a purification factor of 11 in one step using step gradients of NaCl in Tris-HCl buffer at pH 7.5.</p>\",\"PeriodicalId\":20391,\"journal\":{\"name\":\"Preparative biochemistry\",\"volume\":\"21 4\",\"pages\":\"269-75\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1991-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1080/10826069108018578\",\"citationCount\":\"3\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Preparative biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1080/10826069108018578\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Preparative biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1080/10826069108018578","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Purification of prephenate dehydratase from Corynebacterium glutamicum by affinity chromatography.
Prephenate dehydratase has been purified from the wild type strain Corynebacterium glutamicum by affinity chromatography. Three ligands, L-Trp, L-Tyr, and L-Phe have been tested as well as conditions for elution. L-Phe is the most specific ligand: it leads to a purification factor of 11 in one step using step gradients of NaCl in Tris-HCl buffer at pH 7.5.
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