{"title":"Purification and some properties of hemagglutinin from the Myxomycete, Physarum polycephalum.","authors":"M Yokota, K Nitta","doi":"10.1007/BF01969725","DOIUrl":null,"url":null,"abstract":"<p><p>A new hemagglutinin was isolated from the plasmodium of Physarum polycephalum by salting out with ammonium sulphate followed by chromatography on DE-32, DEAE-Toyopearl and hydroxyapatite. This hemagglutinin, named physarumin, was purified 1000-fold over crude extracts. The molecular weight of physarumin was determined to be 22,000 by size exclusion chromatography on Bio-Gel P-60 and 8,700 by SDS-polyacrylamide gel electrophoresis. Physarumin agglutinated rabbit, guinea pig, horse and human erythrocytes. Physarumin-induced hemagglutination was inhibited by fetuin and alpha 1-acid glycoprotein, but not by commercially available mono- and disaccharides. Hemagglutinating activity was blocked by EDTA, and was restored by adding Ca2+ but not by Mg2+.</p>","PeriodicalId":12087,"journal":{"name":"Experientia","volume":"52 6","pages":"544-8"},"PeriodicalIF":0.0000,"publicationDate":"1996-06-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01969725","citationCount":"2","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Experientia","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1007/BF01969725","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 2
Abstract
A new hemagglutinin was isolated from the plasmodium of Physarum polycephalum by salting out with ammonium sulphate followed by chromatography on DE-32, DEAE-Toyopearl and hydroxyapatite. This hemagglutinin, named physarumin, was purified 1000-fold over crude extracts. The molecular weight of physarumin was determined to be 22,000 by size exclusion chromatography on Bio-Gel P-60 and 8,700 by SDS-polyacrylamide gel electrophoresis. Physarumin agglutinated rabbit, guinea pig, horse and human erythrocytes. Physarumin-induced hemagglutination was inhibited by fetuin and alpha 1-acid glycoprotein, but not by commercially available mono- and disaccharides. Hemagglutinating activity was blocked by EDTA, and was restored by adding Ca2+ but not by Mg2+.
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