| 光谱学与光谱分析 |
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| Spectroscopic Study on the Effect of Crystallization of the Hydroxyapatite on the Secondary Structure of Bovine Serum Albumin |
| YE Feng, AN Ying-ge, QIN De-zhi, YANG Lin*,SHE Lan, XING Rui-min |
| College of Chemistry and Environmental Science, Henan Normal University, Xinxiang 453007, China |
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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.
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Received: 2006-02-16
Accepted: 2006-05-28
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Corresponding Authors:
YANG Lin
E-mail: yefeng2003123@163.com*
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| Cite this article: |
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YE Feng,AN Ying-ge,QIN De-zhi, et al. Spectroscopic Study on the Effect of Crystallization of the Hydroxyapatite on the Secondary Structure of Bovine Serum Albumin [J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2007, 27(02): 321-324.
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https://www.gpxygpfx.com/EN/Y2007/V27/I02/321 |
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