This paper used the FTIR method to study the spectra of bovine serum albumin (BSA) and its solution. The secondary structure and conformation was assigned by FTIR-deconvolution analysis. The result indicated that BSA secondary structure in solid is different from in aqueous solution. As the decrease of BSA concentration from 3.241 x 10(-1) to 4.032 X 10(-2) g X mL(-1), the amide I band components at 1 609.84, 1 633.85,1 653.69, 1 681.16 and 1 694.88 cm(-1) shifted to 1 608. 24, 1 638.36, 1 656.10, 1 674.87 and 1 690.78 cm(-1), respectively, the component at 1 621.50 cm(-1) unchanged.