[目的]研究紫花芸豆(Phaseolus vulgaris)胰蛋白酶抑制剂(PVTI)的部分性质.[方法]探索了不同温度、不同还原剂和变性剂处理对PVTI抑制活性和蛋白构象的影响.[结果]PVTI是一种对热稳定蛋白;部分二硫键对活性中心有重要贡献;经尿素处理,PVTI的荧光光谱没有明显变化,但残留了较少的抑制活性,推测亚基的解离影响了抑制活性而每个亚基的内部结构未受到影响;经盐酸胍处理,Trp残基完全暴露于极性环境中,整个蛋白质分子处于一种松散伸展的状态,PVTI活性全部丧失.[结论]该研究可为PVTI的功能研究及其进一步应用奠定基础.%[ Objective ] The research aimed to study the partial characterization of PVTI. [ Method] The inhibitor activity and molecular conformation of PVTI under conditions of different temperature, reducer and denaturant were studied. [ Method] PVTI was a protein of thermal stability. Some disulfide bond was an important necessary for activity. Fluorescence spectrum of PVTI showed unconspicuous changes at 8 mol/L Urea, but it affected active center. Probably It affected inhibitor activity to undo submits, but the inner structure of submits had unconspicuous effects. In the presence of 6 mol/L GlnHCL, tryptophan totally exposed to solvent, molecular conformation was in unwound condition, and PVTI lost all activity. This further proved that tryptophan in nature PVTI located in hydrophobic site of the protein molecular. [Conclusion] The study can lay base for researching PVTI function and its deeply application.
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