目的研究人红细胞内硫氧还蛋白过氧化物酶2(Prx2)与血红蛋白(Hb)的相互作用。方法首先利用红细胞Hb再释放试验分离红细胞和溶血液电泳释放的4个区带,即Hb A、Hb A2、Hb A与Hb A2之间(Hb A-A2)及再释放Hb,将这些区带分别切下,通过反复冻融获得各区带所含蛋白;用葡聚糖G-25浓缩后再利用SDS-PAGE分离各区带所含蛋白组分,并用抗-Prx2做免疫印迹分析;最后用微量热泳动试验(MST)分别检测Prx2蛋白与Hb A和Hb A2之间的结合常数。结果红细胞电泳释放的区带Hb A、Hb A2、Hb A-A2及再释放Hb中均有Prx2;而溶血液电泳释放的Hb区带中,除Hb A2外其余各Hb区带中均有Prx2。MST检测显示,Prx2蛋白与Hb A的结合常数(Kd值)为(14±1.08)μmol/L,而与Hb A2之间的Kd值未被检测到。结论 Prx2与Hb A之间存在相互作用,但与Hb A2之间可能没有相互作用。 Objective To investigate the interaction between human erythrocyte thioredoxin peroxidase 2 (Prx2) and hemoglobin (Hb). Methods Hb reattachment test was used to separate the four bands released by red blood cell and hemolysis electrophoresis, Hb A, Hb A2, Hb A and Hb A2 (Hb A-A2) and then release Hb. These bands Respectively, and the proteins contained in each zone were obtained through repeated freeze-thaw cycles. Protein fractions contained in each zone were concentrated by dextran G-25 and then analyzed by SDS-PAGE. Western blot analysis was performed with anti-Prx2. Finally, The thermophoretic assay (MST) detects the binding constants of Prx2 protein to Hb A and Hb A2, respectively. Results Prx2 was released from Hb A, Hb A2, Hb A-A2 and re-released Hb in erythrocyte electrophoresis. In the Hb band released by hemolytic electrophoresis, Prx2 . MST assay showed that the binding constant (Kd value) of Prx2 protein to Hb A was (14 ± 1.08) μmol / L, while the Kd value with Hb A2 was undetectable. Conclusion There is interaction between Prx2 and Hb A but no interaction with Hb A2.