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在早期对溴酚蓝结合蛋白（ＢＰＢＢＰ）的研究中，我们确定了其在电泳谱中的位置及分子量。目前进行的实验中，我们从不同患者血清中ＢＰＢＢＰ的存在及正常人的血清中ＢＰＢＢＰ的结构和稳定性等方面对ＢＰＢＢＰ进行了测定。测定的结果：（１）在不同患者血清中都不同程度地存在着ＢＰＢＢＰ，这为寻求基因药物载体提供了新思路。（２）不同ｐＨ下，紫外－可见光连续光谱的结果说明ＢＰＢＢＰ与溴酚蓝发生了化学键的结合，并结合稳定；只有当ＢＰＢＢＰ的二级结构被破坏时，方可同溴酚蓝解离；溴酚蓝结构中的发色团也参与了结合，同时ＢＰＢＢＰ与溴酚蓝的结合需要电荷的存在；（３）荧光光谱和荧光淬灭及温度淬灭的结果：ＢＰＢＢＰ中位于分子外部的Ｔｒｐ，Ｔｙｓ，Ｐｈｅ占Ｔｒｐ，Ｔｙｓ，Ｐｈｅ总量的６０％，内部的占４０％；在７５℃时ＢＰＢＢＰ发生热变性，说明ＢＰＢＢＰ的热稳定性较好，这也是基因药物的应用基础之一。
In the early studies of bromophenol blue binding protein (BPBBP), we determined its position and molecular weight in the electropherogram. In the current experiments, we measured BPBBP in the presence of BPBBP in different patient sera and in the structure and stability of BPBBP in normal human serum. The results of the assay: (1) The presence of BPBBP in different patient serums to varying degrees provides a new idea for seeking gene drug carriers. (2) The results of UV-Vis spectra at different pH indicate that BPBBP and bromophenol blue are bound chemically and stably. Only when the secondary structure of BPBBP is destroyed can it dissociate with bromophenol blue. The chromophores in the bromophenol blue structure are also involved in the binding, while the binding of BPBBP to bromophenol blue requires the presence of charge. (3) The results of fluorescence spectroscopy and fluorescence quenching and temperature quenching: Trp outside BPBBP , Tys and Phe account for 60% of the total amount of Trp, Tys and Phe and 40% of the total. The thermal denaturation of BPBBP at 75 ℃ indicates that the thermal stability of BPBBP is better, which is also one of the application bases of gene therapy.