Temperature-sensitive binding of solid phase C1q to aggregated human immunoglobulin G

James J. Gibbons Jr. , Douglas A. Pohl, Cheng C. Tsai, Stanford T. Roodman
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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.

固相C1q与聚集的人免疫球蛋白G的温度敏感结合
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。
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