{"title":"Anti-sDNA antibody purified from sera of human patients with systemic lupus erythematosus—I","authors":"Rita C. Manak , Edward W. Voss Jr.","doi":"10.1016/0161-5890(78)90038-X","DOIUrl":null,"url":null,"abstract":"<div><p>Human SLE sera with anti-nuclear activity were subjected to immunoadsorption with a singlestranded deoxyribonucleic acid (sDNA)-cellulose adsorbant. The antibodies were dissociated from the adsorbant with an equal-molar solution of 4 nucleotides (dAMP. dGMP, dCMP and TMP). Ligand-eluted antibodies were characterized for purity by immunoelectrophoresis and disc gel electrophoresis. Antibody preparations were analyzed for immunoglobulin classes by the capillary precipitin test using class-specific antisera. IgG was the predominant class in all preparations. Purified antibody preparations derived from immunoadsorption were characteristically aggregated as determined by disc-gel electrophoresis and molecular sieve chromatography. The possible sources of aggregation are discussed in detail.</p></div>","PeriodicalId":13265,"journal":{"name":"Immunochemistry","volume":"15 9","pages":"Pages 643-651"},"PeriodicalIF":0.0000,"publicationDate":"1978-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0161-5890(78)90038-X","citationCount":"11","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Immunochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/016158907890038X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 11
Abstract
Human SLE sera with anti-nuclear activity were subjected to immunoadsorption with a singlestranded deoxyribonucleic acid (sDNA)-cellulose adsorbant. The antibodies were dissociated from the adsorbant with an equal-molar solution of 4 nucleotides (dAMP. dGMP, dCMP and TMP). Ligand-eluted antibodies were characterized for purity by immunoelectrophoresis and disc gel electrophoresis. Antibody preparations were analyzed for immunoglobulin classes by the capillary precipitin test using class-specific antisera. IgG was the predominant class in all preparations. Purified antibody preparations derived from immunoadsorption were characteristically aggregated as determined by disc-gel electrophoresis and molecular sieve chromatography. The possible sources of aggregation are discussed in detail.