安徽农业科学2011，Vol.39Issue(16)：9473-9476,4.
紫花芸豆胰蛋白酶抑制剂部分性质研究
Partial Characterization of Trypsin Inhibitor from Phaseolus vulgaris(PVTI)
摘要
Abstract
[ 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.关键词
紫花芸豆/胰蛋白酶抑制剂/荧光光谱/蛋白构象Key words
Phaseolus vulgaris/ Trypsin inhibitor/ Molecular conformation/ Fluorescence spectrum分类
农业科技引用本文复制引用
刘盈盈,杨玲,杨建光,张高..紫花芸豆胰蛋白酶抑制剂部分性质研究[J].安徽农业科学,2011,39(16):9473-9476,4.基金项目
贵州省贵阳市科技局项目(筑科07工00037). （筑科07工00037）
