{"title":"菜豆分离素的快速纯化。","authors":"E Zenteno, M Ortega, Z Qin, J Montreuil, H Debray","doi":"10.1080/10826069408010091","DOIUrl":null,"url":null,"abstract":"<p><p>Phytohemagglutinin from red kidney bean has been purified by affinity chromatography on a human alpha 1-acid glycoprotein Sepharose 4B column. Further purification of the hemagglutinin's five isolectins was achieved on a Mono S column with an 86% protein recovery. Each sequentially eluted isolectin from the ion exchange column displayed either hemagglutinating or mitogenic activity. The main activity of each fraction was the result of the combination of varying proportions of the L and E subunits.</p>","PeriodicalId":20391,"journal":{"name":"Preparative biochemistry","volume":"24 3-4","pages":"175-83"},"PeriodicalIF":0.0000,"publicationDate":"1994-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10826069408010091","citationCount":"3","resultStr":"{\"title\":\"Fast purification of Phaseolus vulgaris isolectins.\",\"authors\":\"E Zenteno, M Ortega, Z Qin, J Montreuil, H Debray\",\"doi\":\"10.1080/10826069408010091\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Phytohemagglutinin from red kidney bean has been purified by affinity chromatography on a human alpha 1-acid glycoprotein Sepharose 4B column. Further purification of the hemagglutinin's five isolectins was achieved on a Mono S column with an 86% protein recovery. Each sequentially eluted isolectin from the ion exchange column displayed either hemagglutinating or mitogenic activity. The main activity of each fraction was the result of the combination of varying proportions of the L and E subunits.</p>\",\"PeriodicalId\":20391,\"journal\":{\"name\":\"Preparative biochemistry\",\"volume\":\"24 3-4\",\"pages\":\"175-83\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1994-11-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1080/10826069408010091\",\"citationCount\":\"3\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Preparative biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1080/10826069408010091\",\"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/10.1080/10826069408010091","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Fast purification of Phaseolus vulgaris isolectins.
Phytohemagglutinin from red kidney bean has been purified by affinity chromatography on a human alpha 1-acid glycoprotein Sepharose 4B column. Further purification of the hemagglutinin's five isolectins was achieved on a Mono S column with an 86% protein recovery. Each sequentially eluted isolectin from the ion exchange column displayed either hemagglutinating or mitogenic activity. The main activity of each fraction was the result of the combination of varying proportions of the L and E subunits.
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