中文摘要：

采用荧光光谱、紫外吸收光谱和圆二色谱（CD）研究了聚乙二醇200基硝苯柳胺与钥孔戚血蓝蛋白（KLH）的相互作用。结果表明，聚乙二醇200基硝苯柳胺对KLH的荧光猝灭机制属于静态猝灭；由Lineweaver—Burk方程计算出不同温度下结合常数K，由Van’t Hoff方程计算出△H和△S平均值，结合力主要为静电作用力；根据FOrster非辐射能量转移机制求得给体与受体间的结合距离r=5．76nm；同步荧光光谱表明，聚乙二醇200基硝苯柳胺能够被KLH存储和转运，但结合时对蛋白的构象有一定的影响；圆二色光谱的数据表明相互作用后KLH的二级结构发生了改变：KLH的α-螺旋的含量从43．1％下降到37．8％。

英文摘要：

The interaction of keyhole limpet hemocyanin （KLH） and PEG200-niphensamide was investigated by fluorescence spectroscopy, ultraviolet absorption spectroscopy and circular dichroism （CD） spectroscopy. It was shown that KLH fluorescence at 340 nm was quenched regularly with the addition of PEG200 niphensamide; the quenching constants were decreased with the temperature increasing; and the quenching was verified as static fluorescence quenching. The binding constants （K） were obtained according to Lineweaver-Burk equation at different temperature. The calculated thermodynamic parameters （ΔH, ΔS） according to Van＇t Hoff equation indicated that the electrostatic interaction played major roles in the binding processes. The distance between KLH and PEG200- niphensamide was 5.76 nm according to the theory of the Forster energy transference. The effects of PEG200 niphensamide on the conformation of KLH were further analyzed by synchronous fluorescence spectroscopy and circular dichroism spectroscopy. PEG200 niphensamide could be deposited and transported by KLH and it affected the conformation of KLH. The secondary structure of KLH was altered （CD data）, i. e. , the a-helices were reduced from 43.1% to 37.8%.