Effect of PbII on the Secondary Structure and Biological Activity of Trypsin

Effect of PbII on the Secondary Structure and Biological Activity of Trypsin
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PbII对胰蛋白酶二级结构和生物活性的影响

DOI:
10.1002/cbic.200400267
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发表时间:
2005-07
期刊:
ChemBioChem,
影响因子:
--
通讯作者:
Xiuying Zhang
Xiuying Zhang
中科院分区:
其他
文献类型:
--
作者:
Lin Yang;Zhiyong Gao;Ying Cao;Ruimin Xing;Xiuying Zhang

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通过监测胰蛋白酶电导率、红外光谱和圆二色性 (CD) 光谱的变化,研究了 PbII 对胰蛋白酶二级结构和生物活性的影响。结果表明,PbII与胰蛋白酶发生反应,结合位点可能是胃蛋白酶中的-OH和-NH基团。 CD 谱表明,与 PbII 的相互作用显着影响胰蛋白酶的二级结构,β 折叠结构含量增加约 42%,而 α 螺旋和 β 转角结构含量分别减少 13% 和 21%。结果清楚地表明,PbII 通过改变胰蛋白酶的二级结构来影响其生物活性。最有趣的是,PbII 在低浓度下上调胰蛋白酶的活性,而在高浓度下下调胰蛋白酶的活性。
The effects of PbII on the secondary structure and biological activity of trypsin have been examined by monitoring changes in its conductivity and IR and circular dichroism (CD) spectra. The results show that PbII reacts with trypsin, and that the binding sites might be OH and NH groups in pepsin. The CD spectra indicate that interaction with PbII significantly affects the secondary structure of trypsin, the β‐sheet‐structure content being increased by about 42 %, whilst those of α‐helix and β‐turn structures are decreased by 13 % and 21 %, respectively. The results clearly demonstrate that PbII affects the biological activity of trypsin by modifying its secondary structure. Most interesting is that PbII up‐regulates the activity of trypsin at low concentrations while down‐regulating it at high concentrations.
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