目的 研究姜黄素（CU）与牛血清白蛋白（BSA）之间的作用机制。方法 采用变温试验研究二者之间的猝灭类型，求算结合数（n）和结合常数。结果 静态猝灭是导致BSA荧光猝灭的主要原因，CU与BSA结合反应的平衡常数（K₀）为5.26×10⁶（21 ℃）和4.60×10⁶（31 ℃），n为1.35。通过计算结合反应的热力学参数，推断CU与BSA之间的作用力以疏水力为主。结论 荧光法适合于研究CU与蛋白质的结合反应，具有简便快速、灵敏度高等优点。

Objective To study the mechanism of interation between curcumin (CU) and bovine serum albumin (BSA). Methods The style of quenching was investigated by changing the reaction temperature. The number and constant of binding sites of CU to BSA were calculated. Results Static quenching was the main reason that caused the quenching of BSA fluorescence. The apparent combining constants (K₀) were 5.26 × 10⁶ at 21 ℃ and 4.60 × 10⁶ at 31 ℃, and the number of binding sites (n) was 1.35. By calculating the thermodynamic parameters, it can be deduced that hydrophobic force is the main binding force between CU and BSA. Conclusion Fluorometric analysis is a good method for the study on CU-BSA binding reaction. It has the advantages of high speed and high sensitivity.