{"title":"[嗜水气单胞菌LP50胞外蛋白水解系统的部分纯化:比较色谱和电泳研究]。","authors":"F Denis, L Veillet-Poncet","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>A complex extracellular proteolytic system was produced by Aeromonas hydrophila LP50 on glucose- polypeptone medium. Partial purification of this system was accomplished by ammonium sulphate precipitation, acetone precipitation, gel filtration on Sephacryl- S200 and chromatography on DEAE-Sephacel. Every stage was controlled by electrophoresis. This proteolytic system was constituted of three aminopeptidase and two endopeptidase components.</p>","PeriodicalId":7904,"journal":{"name":"Annales de microbiologie","volume":"135A 2","pages":"219-27"},"PeriodicalIF":0.0000,"publicationDate":"1984-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[Partial purification of the extracellular proteolytic system of Aeromonas hydrophila LP50: comparative chromatographic and electrophoretic study].\",\"authors\":\"F Denis, L Veillet-Poncet\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>A complex extracellular proteolytic system was produced by Aeromonas hydrophila LP50 on glucose- polypeptone medium. Partial purification of this system was accomplished by ammonium sulphate precipitation, acetone precipitation, gel filtration on Sephacryl- S200 and chromatography on DEAE-Sephacel. Every stage was controlled by electrophoresis. This proteolytic system was constituted of three aminopeptidase and two endopeptidase components.</p>\",\"PeriodicalId\":7904,\"journal\":{\"name\":\"Annales de microbiologie\",\"volume\":\"135A 2\",\"pages\":\"219-27\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1984-03-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Annales de microbiologie\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Annales de microbiologie","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
[Partial purification of the extracellular proteolytic system of Aeromonas hydrophila LP50: comparative chromatographic and electrophoretic study].
A complex extracellular proteolytic system was produced by Aeromonas hydrophila LP50 on glucose- polypeptone medium. Partial purification of this system was accomplished by ammonium sulphate precipitation, acetone precipitation, gel filtration on Sephacryl- S200 and chromatography on DEAE-Sephacel. Every stage was controlled by electrophoresis. This proteolytic system was constituted of three aminopeptidase and two endopeptidase components.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
