Bhattacharyya M, Chaudhuri U, Poddar R K
Department of Biophysics, Molecular Biology and Genetics, University of Calcutta, India.
Int J Biol Macromol. 1990 Oct;12(5):297-301. doi: 10.1016/0141-8130(90)90017-5.
The interaction of chlorpromazine (CPZ), a widely used antipsychotic tranquillizer, with the allosteric protein haemoglobin, has been studied by different methods. From r versus Cf plot obtained by an equilibrium dialysis experiment, the maximum value of r was found to be 6.8 at 0.15 M NaCl. Binding parameters, namely the affinity constant K and the degree of cooperativity nH, were determined from the Hill plot. Circular dichroism studies indicate a conformation change of haemoglobin in the presence of CPZ. Oxygen has been found to be released from haemoglobin with the progressive addition of CPZ. The extent of the release of oxygen depends on the stoichiometric ratio of CPZ: haemoglobin (D/P). The possible nature of the binding site of the protein has been discussed on the basis of the information obtained from fluorescence measurements.
广泛使用的抗精神病镇静剂氯丙嗪（CPZ）与变构蛋白血红蛋白的相互作用已通过不同方法进行了研究。从平衡透析实验获得的r对Cf图中，发现在0.15 M NaCl条件下r的最大值为6.8。结合参数，即亲和常数K和协同度nH，由希尔图确定。圆二色性研究表明在CPZ存在下血红蛋白的构象发生了变化。已发现随着CPZ的逐步添加，氧气从血红蛋白中释放出来。氧气的释放程度取决于CPZ与血红蛋白的化学计量比（D/P）。已根据从荧光测量获得的信息讨论了蛋白质结合位点的可能性质。
