曙红Y在牛血清白蛋白表面上的Langmuir吸附反应研究

Langmuir aggregation of Eosin Y in protein macromolecule

应用微相吸附-光谱修正技术研究了曙红Y(EY)与牛血清白蛋白(BSA)的相互作用,并讨论了反应时间、离子强度、温度,以及金属离子干扰等因素对该作用产生的影响.结果表明,EY与BSA间的作用符合Langmuir单分子层吸附,结合产物最大结合数NEY∶NBSA=5∶1;计算了不同温度下(30,45和60℃)反应的结合常数K,发现K随温度的升高而减小;并测定了蛋白质的工作曲线,该方法的检出限为20 mg/L.

The interaction between Eosin Y（EY） and bovine serum albumin（BSA） has been investigated by microphase adsorption-spectral correction（MPASC） technique.EY could be absorbed on the protein by electrostatic force and the aggregation obeyed the Langmuir isothem.Results showed that the adsorption ration（N） of EY to BSA was about 5∶ 1,the adsorption constant（K） was 2.34×10^5（30 ℃）,and the value of K decreased when the temperature increased.We also disscussed the effect of ionic strength and metal ions on the interaction in this paper.