{"title":"【色谱分离后大肠杆菌酯酶B的表征】。","authors":"P Goullet, B Picard, H S Hieng","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Esterase B of Escherichia coli has been purified 56 fold with recovery of 39%. The apparent molecular weight as determined by gel filtration was approximately 57000. The pI as determined by isoelectric focusing was 4.6. This enzyme exhibited Michaelis-Menton kinetics with apparent Km of 0.25 mM for l-naphtyl acetate. It remained stable at 60 degrees C but was sensitive to pH values below 6. The esterase activity was completely inhibited by Di-isopropyl-fluorophosphate (DFP) but was resistant to iodoacetamide and to EDTA.</p>","PeriodicalId":10622,"journal":{"name":"Comptes rendus des seances de l'Academie des sciences. Serie III, Sciences de la vie","volume":"296 4","pages":"177-80"},"PeriodicalIF":0.0000,"publicationDate":"1983-01-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[Characterization of Escherichia coli esterase B after separation by chromatography].\",\"authors\":\"P Goullet, B Picard, H S Hieng\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Esterase B of Escherichia coli has been purified 56 fold with recovery of 39%. The apparent molecular weight as determined by gel filtration was approximately 57000. The pI as determined by isoelectric focusing was 4.6. This enzyme exhibited Michaelis-Menton kinetics with apparent Km of 0.25 mM for l-naphtyl acetate. It remained stable at 60 degrees C but was sensitive to pH values below 6. The esterase activity was completely inhibited by Di-isopropyl-fluorophosphate (DFP) but was resistant to iodoacetamide and to EDTA.</p>\",\"PeriodicalId\":10622,\"journal\":{\"name\":\"Comptes rendus des seances de l'Academie des sciences. Serie III, Sciences de la vie\",\"volume\":\"296 4\",\"pages\":\"177-80\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1983-01-31\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Comptes rendus des seances de l'Academie des sciences. Serie III, Sciences de la vie\",\"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":"Comptes rendus des seances de l'Academie des sciences. Serie III, Sciences de la vie","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
[Characterization of Escherichia coli esterase B after separation by chromatography].
Esterase B of Escherichia coli has been purified 56 fold with recovery of 39%. The apparent molecular weight as determined by gel filtration was approximately 57000. The pI as determined by isoelectric focusing was 4.6. This enzyme exhibited Michaelis-Menton kinetics with apparent Km of 0.25 mM for l-naphtyl acetate. It remained stable at 60 degrees C but was sensitive to pH values below 6. The esterase activity was completely inhibited by Di-isopropyl-fluorophosphate (DFP) but was resistant to iodoacetamide and to EDTA.
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