James J. Gibbons Jr. , Douglas A. Pohl, Cheng C. Tsai, Stanford T. Roodman
{"title":"Temperature-sensitive binding of solid phase C1q to aggregated human immunoglobulin G","authors":"James J. Gibbons Jr. , Douglas A. Pohl, Cheng C. Tsai, Stanford T. Roodman","doi":"10.1016/0005-2795(81)90002-7","DOIUrl":null,"url":null,"abstract":"<div><p>The first component of complement (C1q) coupled to Sepharose by cyanogen bromide was found not to bind aggregated human γ-globulin or immune complexes at room temperature, whereas at 4°C binding was nearly complete. The temperature sensitivity of solid phase C1q binding was reversible. Elution of aggregated human γ-globulin bound at 4°C was possible by raising the temperature to 23°C. However, free C1q or C1q adsorbed onto polystyrene balls could bind immune complex-like material at both 23 and 4°C. The conformational restraints of C1q covalently coupled to a solid support may not allow functional activity at elevated temperatures.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"670 2","pages":"Pages 146-149"},"PeriodicalIF":0.0000,"publicationDate":"1981-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90002-7","citationCount":"2","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Protein Structure","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0005279581900027","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
The first component of complement (C1q) coupled to Sepharose by cyanogen bromide was found not to bind aggregated human γ-globulin or immune complexes at room temperature, whereas at 4°C binding was nearly complete. The temperature sensitivity of solid phase C1q binding was reversible. Elution of aggregated human γ-globulin bound at 4°C was possible by raising the temperature to 23°C. However, free C1q or C1q adsorbed onto polystyrene balls could bind immune complex-like material at both 23 and 4°C. The conformational restraints of C1q covalently coupled to a solid support may not allow functional activity at elevated temperatures.