K. Teramoto, Y. Nakamoto, T. Kunitomo, H. Shoji, T. Tani, K. Hanazawa, M. Kodama
{"title":"Removal of endotoxin in blood by polymyxin B immobilized polystyrene-derivative fiber.","authors":"K. Teramoto, Y. Nakamoto, T. Kunitomo, H. Shoji, T. Tani, K. Hanazawa, M. Kodama","doi":"10.1046/J.1526-0968.2002.00411.X","DOIUrl":null,"url":null,"abstract":"Polymyxin B, a cationic cyclic decapeptide antibiotic, is well known to bind endotoxin and to neutralize its toxicity. Based on this principle, polymyxin B was immobilized on the chloroacetamidomethylated polystyrene fiber that is reinforced by polypropylene. The adsorbing capacity of the obtained fibers (polymyxin B immobilized fiber [PMX-F]) was evaluated on endotoxin and other serum components in serum and on heparin in phosphate-buffered saline. Fluorescein isothiocyanate-labeled or tetramethylrhodamine isothiocyanate-labeled lipopolysaccharide (LPS) was used as endotoxin. The measurement of the fluorescence intensity showed that PMX-F adsorbed these LPSs depending on their concentration and on amount. The adsorption of endotoxin was confirmed by desorption of LPS from PMX-F as well. PMX-F adsorbed serum amyloid protein A besides LPS, but neither C-reactive protein nor low-density lipoprotein. The adsorbing property of heparin was low.","PeriodicalId":79755,"journal":{"name":"Therapeutic apheresis : official journal of the International Society for Apheresis and the Japanese Society for Apheresis","volume":"11 1","pages":"103-8"},"PeriodicalIF":0.0000,"publicationDate":"2002-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"14","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Therapeutic apheresis : official journal of the International Society for Apheresis and the Japanese Society for Apheresis","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1046/J.1526-0968.2002.00411.X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 14
Abstract
Polymyxin B, a cationic cyclic decapeptide antibiotic, is well known to bind endotoxin and to neutralize its toxicity. Based on this principle, polymyxin B was immobilized on the chloroacetamidomethylated polystyrene fiber that is reinforced by polypropylene. The adsorbing capacity of the obtained fibers (polymyxin B immobilized fiber [PMX-F]) was evaluated on endotoxin and other serum components in serum and on heparin in phosphate-buffered saline. Fluorescein isothiocyanate-labeled or tetramethylrhodamine isothiocyanate-labeled lipopolysaccharide (LPS) was used as endotoxin. The measurement of the fluorescence intensity showed that PMX-F adsorbed these LPSs depending on their concentration and on amount. The adsorption of endotoxin was confirmed by desorption of LPS from PMX-F as well. PMX-F adsorbed serum amyloid protein A besides LPS, but neither C-reactive protein nor low-density lipoprotein. The adsorbing property of heparin was low.