羟基磷灰石-碳酸钙-BSA水溶性复合物中蛋白质微观结构的研究

Study on the Microstructure of Protein in Soluble Complexes Containing Bovine Serum Albumin and Calcium Hydroxyapatite and Calcium Carbonate

利用傅里叶变换红外光谱 ,结合二阶导数谱、退卷积和曲线拟合等计算机解析方法 ,对牛血清白蛋白(BSA) 羟基磷灰石 碳酸钙水溶性复合物中BSA的二级结构进行了研究。结果表明 ,BSA的α 螺旋结构的含量增加 ,蛋白质结构趋于有序化 ;紫外光谱和紫外二阶导数谱的研究发现 ,BSA的芳香族氨基酸残基的微环境受到扰动。在生物体内 ,正是蛋白质结构的这些变化导致生物矿化过程的发生和进行。

FTIR spectra and ultraviolet spectra with derivation, deconvolution and curve-fitting methods were used to study the microstructure of bovine serum albumin (BSA) in the soluble complexes containing bovine serum albumin (BSA) and calcium hydroxyapatite and calcium carbonate. The result demonstrates that the alpha-helix structure of BSA increases and the microenvironment of the aromatic amino acid residues changes, which are helpful for the biomineralization process in organism.