Teppo A M, Wager O
Scand J Immunol. 1979;10(5):431-5. doi: 10.1111/j.1365-3083.1979.tb01372.x.
The effect of heating at 56 degrees C on free and complex-bound Clq was studied by radioisotope and sucrose gradient centrifugation techniques. The ability of soluble complexes of egg albumin, rabbit anti-egg albumin, and human Clq to bind extrinsic iodinated Clq did not increase following heating at 56 degrees C. The results of this study did not support the postulated release of complex-bound Clq on heating at 56 degrees C. They also showed that free Clq was more heat-labile than Clq in the Clqrs state. The importance of elimination or monitoring of intrinsic Clq in Clq assays for circulating immune complexes is stressed.
通过放射性同位素和蔗糖梯度离心技术研究了56℃加热对游离和与复合物结合的Clq的影响。卵清蛋白、兔抗卵清蛋白和人Clq的可溶性复合物结合外源性碘化Clq的能力在56℃加热后并未增加。本研究结果不支持56℃加热时复合物结合的Clq会释放的假设。研究还表明，游离Clq比处于Clqrs状态的Clq更不耐热。强调了在循环免疫复合物的Clq检测中消除或监测内源性Clq的重要性。
