[Objective]The aim was to study the interaction characteristic of bovine serum albumin (BSA) and carbofuran. [Method]With synchronous fluorescence spectrometry adopted, the interaction of carbofuran and BSA in Tris-HCl buffer system (pH 7.40) was investigated. The binding constants at different temperatures were calculated and the interaction types between carbofuran and BSA were discussed.[Result]Under normal physiological conditions, higher quenching effect of carbofuran on BSA was electrostatic interaction. The changes of different drug concentrations and temperature proved a static quenching of carbofuran with BSA. The binding constants (KSV) at 25 °C, 37 °C and 50 °C were 1.17×104, 1.07×104 and 0.99×104 L/mol respectively with ratio of carbofuran and BSA at 1∶1.[Conclusion]The research is of guiding significance for learning transport and metabolism of carbofuran at molecular level. [Objective] The aim was to study the interaction characteristic of bovine serum albumin (BSA) and carbofuran. [Method] With synchronous fluorescence spectrometry adopted, the interaction of carbofuran and BSA in Tris-HCl buffer system (pH 7.40) was investigated. binding constants at different temperatures were calculated and the interaction types between carbofuran and BSA were discussed. [Result] Under normal physiological conditions, higher quenching effect of carbofuran on BSA was electrostatic interaction. The changes of different drug concentrations and temperature proved a static quenching of The binding constants (KSV) at 25 ° C, 37 ° C and 50 ° C were 1.17 × 104, 1.07 × 104 and 0.99 × 104 L / mol respectively with carbofuran and BSA at 1: 1. [ Conclusion] The research is of guiding significance for learning transport and metabolism of carbofuran at molecular level.