{"title":"Isolation and partial characterization of two isolectins from Lathyrus ochrus (L.) DC. seeds","authors":"Pierre Rougé , Benildo Sousa-Cavada","doi":"10.1016/0304-4211(84)90197-4","DOIUrl":null,"url":null,"abstract":"<div><p>Two isolectins have been isolated from <em>Lathyrus ochrus</em> (L.) DC. seeds by ammonium sulfate precipitation, affinity chromatography on Sephadex G-100 and subsequent chromatofocusing. The isolectins, whose isoelectric points are respectively pH 7.2 and pH 6.0, have a relative molecular mass about 49 000 and are tetramers consisting of two slightly different kinds of light (<em>M</em><sub><em>r</em></sub> 4500) and heavy (<em>M</em><sub><em>r</em></sub> 20 000) subunits. The amino acid composition, N-terminal amino acids, carbohydrate and metal content of both the isolectins and their subunits have been compared. The isolectins are non-specific in hemagglutination and agglutinate equally well human erythrocytes of different ABO groups. Their hemagglutinating activity is inhibited best by D-mannose, D-glucose and their α-methylglucosides derivatives. They share antigenic determinants in common with other <em>Lathyrus</em> lectins and other lectins belonging to the <em>Vicieae</em> tribe.</p></div>","PeriodicalId":20221,"journal":{"name":"Plant Science Letters","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1984-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0304-4211(84)90197-4","citationCount":"29","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Plant Science Letters","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0304421184901974","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 29
Abstract
Two isolectins have been isolated from Lathyrus ochrus (L.) DC. seeds by ammonium sulfate precipitation, affinity chromatography on Sephadex G-100 and subsequent chromatofocusing. The isolectins, whose isoelectric points are respectively pH 7.2 and pH 6.0, have a relative molecular mass about 49 000 and are tetramers consisting of two slightly different kinds of light (Mr 4500) and heavy (Mr 20 000) subunits. The amino acid composition, N-terminal amino acids, carbohydrate and metal content of both the isolectins and their subunits have been compared. The isolectins are non-specific in hemagglutination and agglutinate equally well human erythrocytes of different ABO groups. Their hemagglutinating activity is inhibited best by D-mannose, D-glucose and their α-methylglucosides derivatives. They share antigenic determinants in common with other Lathyrus lectins and other lectins belonging to the Vicieae tribe.