James J. Gibbons Jr. , Douglas A. Pohl, Cheng C. Tsai, Stanford T. Roodman
{"title":"固相C1q与聚集的人免疫球蛋白G的温度敏感结合","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":"{\"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}","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}
Temperature-sensitive binding of solid phase C1q to aggregated human immunoglobulin G
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.