固相C1q与聚集的人免疫球蛋白G的温度敏感结合

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. ,&nbsp;Douglas A. Pohl,&nbsp;Cheng C. Tsai,&nbsp;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. ,&nbsp;Douglas A. Pohl,&nbsp;Cheng C. Tsai,&nbsp;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}
引用次数: 2

摘要

通过溴化氰与Sepharose偶联的补体第一组分(C1q)在室温下不与聚集的人γ-球蛋白或免疫复合物结合,而在4℃时几乎完全结合。固相C1q结合的温度敏感性是可逆的。将温度提高到23°C,可以在4°C下洗脱聚集的人γ-球蛋白。然而,吸附在聚苯乙烯球上的游离C1q或C1q可以在23°C和4°C下结合免疫复合物样材料。共价耦合到固体载体的C1q的构象限制可能不允许在高温下的功能活性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信