The interaction between ascorbic acid(AA)and bovine serum albumin(BSA)was investigated us⁃ing the self-made modified electrode by cyclic voltammetry and fluorescence. The binding constants of 1.761×104 L/mol and 1.884×104 L/mol can be calculated from the data obtained from fluorescence quenching experiments and cyclic voltammetry,respectively. And the number of the binding sites is nearly 1.0. The in⁃teraction of bovine serum albumin with AA was a single static quenching procedure. Within the limits ,the fluorescence intensity changes BSA linearly with the concentrations of AA,the linear range is 2.50 × 10-7~3.50×10-4 mol/L,and the detection limit is 1.0×10-7 mol/L. Within the limits,the redox peak current of AA was proportional to the the concentration of BSA,the linear range is 2.50×10-8~5.00×10-5mol/L,and the de⁃tection limit is 1.0×10-9 mol/L. It has been applied to the determination BSA and AA in the samples with sat⁃isfactory results.%用自制修饰电极通过循环伏安法和荧光法，分别研究牛血清白蛋白与抗坏血酸的相互作用.用循环伏安法和荧光法测得抗坏血酸与牛血清白蛋白的结合常数K分别为1.761×104 L/mol和1.884×104 L/mol，结合位点数均接近1.0.实验测得抗坏血酸对牛血清白蛋白是静态猝灭.抗坏血酸浓度与牛血清白蛋白荧光强度的降低在2.50×10-7~3.50×10-4 mol/L范围内呈线性关系，检出限为1.0×10-7 mol/L.牛血清白蛋白浓度与抗坏血酸氧化峰电流的下降在2.50×10-8~5.00×10-5 mol/L范围内呈线性关系，检出限为1.0×10-9 mol/L.此法用于样品中抗坏血酸和牛血清白蛋白的测定，结果满意.
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