牛血清白蛋白二级结构构象的红外光谱研究(英文)

A Study of Secondary Structural Conformation of Bovine Serum Albumin by FTIR

研究了BSA(bovineserumalbumin,牛血清白蛋白 )及其水溶液的红外光谱 ,通过傅里叶自转积谱分析 ,对上述红外光谱的二级结构构象进行了指认。结果表明 ,BSA处于水溶液状态与固态时的二级结构是不同的。随着溶液浓度的降低 ( 3.2 4 1× 1 0 -1～ 4 .0 32× 1 0 -2 g·ml-1),酰胺I带二级结构子峰存在明显的位移现象 ,即 1 6 0 9.86cm-1位移到 1 6 0 8.2 4cm-1,1 6 33.85位移到 1 6 38.36cm-1,1 6 53.6 9cm-1位移到 1 6 56 .1 0cm-1,1 6 81.1 6cm-1位移到1 6 74 .87cm-1,1 6 94.88cm-1位移到 1 6 90 .78cm-1,而 1 6 2 1 .

In this paper,the Fourier Transformation Infrared spectrum (FTIR) method was used 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 in aqueous solution. As the decrease of BSA concentration from 3.241×10 -1 to 4.032×10 -2 g·ml -1 ,the amide I band components at 1609.84,1633.85,1653.69,1681.16 and 1694.88cm -1 shifted to 1608.24,1638.36,1656.10,1674.87 and 1690.78cm -1 ,respectively, the component at 1621.50cm -1 unchanged.