Abstract：The effect of crystallization of hydroxyapatite on the secondary structure of bovine serum albumin(BSA) was studied by circular dichroism spectrum, Fourier transform infrared spectroscopy, derivative, deconvolution and curve-fitting techniques in the present paper. The CD results show that pure bovine serum albumin is composed of 56.8% α-helices, 5.8% β-sheets, 14.1% β-turns and 23.9% random structures, while the bovine serum albumin in the Ca10(PO4)6(OH)2/bovine serum albumin solution is composed of 25.4% α-helices, 25.0% β-sheets, 20.0% β-turns and 29.7% random structures. The results of Fourier transform infrared spectroscopy are in good agreement with those from the CD spectra. From these results it can be seen that the percentage of α-helix decreased, while that of the β-sheet increased with the formation of the crystal of hydroxyapatite, and with the reaction time increasing, the percentages of α-helix obviously dropped and those of β-sheet markedly rose. These results showed that α-helix transformed into β-sheet. Furthermore the essence of these changes is discussed.
叶锋,安英格,秦德志,杨林*,佘岚,邢瑞敏. 羟基磷灰石结晶对牛血清白蛋白二级结构影响的光谱研究[J]. 光谱学与光谱分析, 2007, 27(02): 321-324.
YE Feng, AN Ying-ge, QIN De-zhi, YANG Lin*,SHE Lan, XING Rui-min . Spectroscopic Study on the Effect of Crystallization of the Hydroxyapatite on the Secondary Structure of Bovine Serum Albumin . SPECTROSCOPY AND SPECTRAL ANALYSIS, 2007, 27(02): 321-324.
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