{"title":"Inverse-gradient polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate for better separation of protein samples","authors":"M. Hashiguchi, K. Shimizu, T. Hashiguchi","doi":"10.2198/JELECTROPH.55.1","DOIUrl":null,"url":null,"abstract":"We found that the relationship between the molecular mass of a protein and its mobility in polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate on an inverse-gradient (15-5%) gel is linear on a double logarithmic plot. In contrast, this relationship is not linear for proteins resolved on a standard 10% gel, but is fitted to two straight lines. Both gel types gave a similar slope in resolving proteins smaller than 100 kDa but inverse-gradient (15-5%) gel separated proteins with wider range of molecular mass. On the other hand, the standard 10% gel provided better separation of proteins larger than 100 kDa. These results suggest that the 15-5% inverse-gradient gel is best suited for the separation of proteins smaller than 100 kDa. The advantage of inverse-gradient gel SDS-PAGE may stem from the fact that unstacking of SDS-protein complexes in inverse-gradient gels is faster and more complete than in standard 10% gels.","PeriodicalId":15059,"journal":{"name":"Journal of capillary electrophoresis","volume":"66 1","pages":"1-3"},"PeriodicalIF":0.0000,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of capillary electrophoresis","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2198/JELECTROPH.55.1","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 1
Abstract
We found that the relationship between the molecular mass of a protein and its mobility in polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate on an inverse-gradient (15-5%) gel is linear on a double logarithmic plot. In contrast, this relationship is not linear for proteins resolved on a standard 10% gel, but is fitted to two straight lines. Both gel types gave a similar slope in resolving proteins smaller than 100 kDa but inverse-gradient (15-5%) gel separated proteins with wider range of molecular mass. On the other hand, the standard 10% gel provided better separation of proteins larger than 100 kDa. These results suggest that the 15-5% inverse-gradient gel is best suited for the separation of proteins smaller than 100 kDa. The advantage of inverse-gradient gel SDS-PAGE may stem from the fact that unstacking of SDS-protein complexes in inverse-gradient gels is faster and more complete than in standard 10% gels.