{"title":"钙调素亲和层析纯化大大麻乳胶过氧化物酶。","authors":"Francesca Pintus, Anna Mura","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>A new procedure to purify to homogeneity an Euphorbia characias latex peroxidase is performed employing a calmodulin-Sepharose column as affinity chromatography. The advantage of this approach is the isolation of a peroxidase under fast and mild elution conditions with a high recovery in total activity.</p>","PeriodicalId":22527,"journal":{"name":"The Italian journal of biochemistry","volume":"56 1","pages":"1-5"},"PeriodicalIF":0.0000,"publicationDate":"2007-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Purification of Euphorbia characias latex peroxidase by calmodulin-affinity chromatography.\",\"authors\":\"Francesca Pintus, Anna Mura\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>A new procedure to purify to homogeneity an Euphorbia characias latex peroxidase is performed employing a calmodulin-Sepharose column as affinity chromatography. The advantage of this approach is the isolation of a peroxidase under fast and mild elution conditions with a high recovery in total activity.</p>\",\"PeriodicalId\":22527,\"journal\":{\"name\":\"The Italian journal of biochemistry\",\"volume\":\"56 1\",\"pages\":\"1-5\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2007-03-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"The Italian journal of biochemistry\",\"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":"The Italian journal of biochemistry","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Purification of Euphorbia characias latex peroxidase by calmodulin-affinity chromatography.
A new procedure to purify to homogeneity an Euphorbia characias latex peroxidase is performed employing a calmodulin-Sepharose column as affinity chromatography. The advantage of this approach is the isolation of a peroxidase under fast and mild elution conditions with a high recovery in total activity.
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