Effects of Two Trypsin Inhibitors on Trypsin in Activity and Structure

机译：两种胰蛋白酶抑制剂对活动与结构胰蛋白酶的影响

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Two reversible trypsin inhibitors, Kunitz trypsin inhibitor (KTI) and Bowman-Birk trypsin inhibitor (BBI) were compared to find the more optimal one as the inhibit factor during trypsin immobilization. Fluorescence spectroscopy, UV-visible absorption spectroscopy and circular dichroism (CD) spectroscopy were used to explore the effects of the two inhibitors on trypsin in activity and structure. The results showed that both inhibitors combined with trypsin in 1:1. CD circular dichroism spectroscopy showed that KTI and BBI led to different changes in trypsin second structure. The results can help us find out the mechanism between the two inhibitors and trypsin and select the more optimal inhibitor in trypsin immobilization.

机译：比较两种可逆胰蛋白酶抑制剂，Kunitz胰蛋白酶抑制剂（KTI）和Bowman-Birk胰蛋白酶抑制剂（BBI），以发现更优选的是胰蛋白酶固定期间的抑制因子。荧光光谱法，UV可见吸收光谱和圆形二色性（CD）光谱用于探讨两种抑制剂对活性和结构胰蛋白酶的影响。结果表明，两种抑制剂与胰蛋白酶合并1：1。 CD圆形二色性光谱显示KTI和BBI导致胰蛋白酶第二结构的不同变化。结果可以帮助我们发现两种抑制剂和胰蛋白酶之间的机制，并在胰蛋白酶固定中选择更良好的抑制剂。

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《International Conference on Energy, Environment and Sustainable Development》|2015年||共4页
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作者
Shuting Dong; Hong Zhuang; Na Xu;
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中图分类 TB3-532;
关键词
Trypsin; KTI; BBI; Interaction.;

机译：胰蛋白酶;KTI;BBI;互动。;

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机译：肝素对人尿胰蛋白酶抑制剂（Ulinastatin）对胰蛋白酶，胰凝乳蛋白酶和白细胞弹性蛋白酶抑制活性的影响
2. The electrostatic interactions between nano-TiO(2) and trypsin inhibit the enzyme activity and change the secondary structure of trypsin. [J] . Wang WR, Zhu RR, Xiao R, Biological trace element research . 2011,第3期

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3. The Electrostatic Interactions Between Nano-TiO₂ and Trypsin Inhibit the Enzyme Activity and Change the Secondary Structure of Trypsin [J] . Wen-Rui Wang, Rong-Rong Zhu, Rong Xiao, Biological Trace Element Research . 2011,第3期

机译：纳米TiO _{2 与胰蛋白酶的静电相互作用抑制酶活性并改变胰蛋白酶的二级结构}
4. Effects of Two Trypsin Inhibitors on Trypsin in Activity and Structure [C] . Shuting Dong, Hong Zhuang, Na Xu International Conference on Energy, Environment and Sustainable Development . 2015

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6. Crystal structures of bovine chymotrypsin and trypsin complexed to the inhibitor domain of Alzheimers amyloid beta-protein precursor (APPI) and basic pancreatic trypsin inhibitor (BPTI): engineering of inhibitors with altered specificities. [O] . A. J. Scheidig, T. R. Hynes, L. A. Pelletier, 1997

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Effects of Two Trypsin Inhibitors on Trypsin in Activity and Structure

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