【摘要】 通过圆二色谱(CD)及傅里叶变换红外光谱及退卷积、曲线拟合等技术研究了羟基磷灰石结晶对牛血清白蛋白二级结构的影响。CD谱结果表明,在纯的牛血清白蛋白中,α-螺旋、β-折叠、β-转角及无规则卷曲等4种结构的含量分别为56.8%,5.8%,14.1%,23.9%;而在羟基磷灰石/牛血清白蛋白溶液中,4种结构的含量分别为25.4%,25.0%,20.0%和29.7%,红外光谱结果与其一致。由此可以看出,晶体的形成使牛血清白蛋白的α-螺旋结构含量减少,β-折叠结构含量增多,且随着反应时间的进行α-螺旋结构减少越来越明显,β-折叠结构增加越来越多,表明在溶液中部分α-螺旋结构转变为β-折叠结构。文章对这种变化的本质进行了初步探讨。更多还原

【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.更多还原