{"title":"金黄色葡萄球菌细胞外蛋白A与辛基-sepharose CL-4B的疏水相互作用。","authors":"R Varró, A Jagicza","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Extracellular Protein A from Staphylococcus aureus was shown to bind to alkyl agarose adsorbents of different carbon chain length. Octyl-Sepharose CL-4B was chosen to purify the active material, as the strong interaction with this adsorbent allowed the separation of Protein A from the bulk of the contaminants. Protein A retained its ability to bind to IgG in the presence of up to 3.5 M ethylene glycol as demonstrated by hemagglutination. A theory on the possible involvement of hydrophobic interaction in the binding reaction of Protein A to IgG is advanced.</p>","PeriodicalId":7910,"journal":{"name":"Annales immunologiae Hungaricae","volume":"19 ","pages":"79-84"},"PeriodicalIF":0.0000,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Hydrophobic interaction of extracellular protein A from Staphylococcus aureus with octyl-sepharose CL-4B.\",\"authors\":\"R Varró, A Jagicza\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Extracellular Protein A from Staphylococcus aureus was shown to bind to alkyl agarose adsorbents of different carbon chain length. Octyl-Sepharose CL-4B was chosen to purify the active material, as the strong interaction with this adsorbent allowed the separation of Protein A from the bulk of the contaminants. Protein A retained its ability to bind to IgG in the presence of up to 3.5 M ethylene glycol as demonstrated by hemagglutination. A theory on the possible involvement of hydrophobic interaction in the binding reaction of Protein A to IgG is advanced.</p>\",\"PeriodicalId\":7910,\"journal\":{\"name\":\"Annales immunologiae Hungaricae\",\"volume\":\"19 \",\"pages\":\"79-84\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1979-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Annales immunologiae Hungaricae\",\"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":"Annales immunologiae Hungaricae","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Hydrophobic interaction of extracellular protein A from Staphylococcus aureus with octyl-sepharose CL-4B.
Extracellular Protein A from Staphylococcus aureus was shown to bind to alkyl agarose adsorbents of different carbon chain length. Octyl-Sepharose CL-4B was chosen to purify the active material, as the strong interaction with this adsorbent allowed the separation of Protein A from the bulk of the contaminants. Protein A retained its ability to bind to IgG in the presence of up to 3.5 M ethylene glycol as demonstrated by hemagglutination. A theory on the possible involvement of hydrophobic interaction in the binding reaction of Protein A to IgG is advanced.