{"title":"精氨酸溶液中蛋白质的多模态色谱法(01C)。蛋白质:性质,海报,第52届日本生物物理学会年会(BSJ2014)","authors":"A. Hirano, T. Arakawa, T. Kameda","doi":"10.2142/BIOPHYS.54.S257_1","DOIUrl":null,"url":null,"abstract":"Arginine is effective in elution of proteins from chromatography columns. In this study, effects of arginine on the elution from multimodal chromatography columns, the resins of which have multiple functional groups, were examined using bovine serum albumin and a monoclonal antibody against interleukin-8. The resins used here were Capto MMC and Capto adhere, which are multimodal cation and anion exchangers, respectively. As expected, arginine effectively eluted the proteins from the columns. Mechanism of the elution was examined by molecular dynamics simulations. The results showed that the affinity of arginine was primarily associated with electrostatic interaction for Capto MMC and with hydrophobic and π-π interactions as well as hydrogen bonding for Capto adhere.","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"18 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2014-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"3P049 Multimodal chromatography of proteins in arginine solutions(01C. Protein: Property,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))\",\"authors\":\"A. Hirano, T. Arakawa, T. Kameda\",\"doi\":\"10.2142/BIOPHYS.54.S257_1\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Arginine is effective in elution of proteins from chromatography columns. In this study, effects of arginine on the elution from multimodal chromatography columns, the resins of which have multiple functional groups, were examined using bovine serum albumin and a monoclonal antibody against interleukin-8. The resins used here were Capto MMC and Capto adhere, which are multimodal cation and anion exchangers, respectively. As expected, arginine effectively eluted the proteins from the columns. Mechanism of the elution was examined by molecular dynamics simulations. The results showed that the affinity of arginine was primarily associated with electrostatic interaction for Capto MMC and with hydrophobic and π-π interactions as well as hydrogen bonding for Capto adhere.\",\"PeriodicalId\":409321,\"journal\":{\"name\":\"Seibutsu Butsuri\",\"volume\":\"18 1\",\"pages\":\"0\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2014-08-20\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Seibutsu Butsuri\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.2142/BIOPHYS.54.S257_1\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Seibutsu Butsuri","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2142/BIOPHYS.54.S257_1","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
3P049 Multimodal chromatography of proteins in arginine solutions(01C. Protein: Property,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))
Arginine is effective in elution of proteins from chromatography columns. In this study, effects of arginine on the elution from multimodal chromatography columns, the resins of which have multiple functional groups, were examined using bovine serum albumin and a monoclonal antibody against interleukin-8. The resins used here were Capto MMC and Capto adhere, which are multimodal cation and anion exchangers, respectively. As expected, arginine effectively eluted the proteins from the columns. Mechanism of the elution was examined by molecular dynamics simulations. The results showed that the affinity of arginine was primarily associated with electrostatic interaction for Capto MMC and with hydrophobic and π-π interactions as well as hydrogen bonding for Capto adhere.