复杂基质中胰蛋白酶抑制活性的定量测定

R. Spelbrink, P. Gerrits, C. Mooij, M. Giuseppin
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引用次数: 9

摘要

利用偶氮酪蛋白进行定量分析,以测量乳剂和其他难以分析的复杂系统中的胰蛋白酶抑制活性。该方法在纯蛋白质溶液以及富含脂肪和糖的含蛋白质物质上进行了重复性测试,特别注意乳剂。在清洁情况下,总体相对标准偏差小于6%,而对于更复杂的系统,其相对标准偏差小于16%。实验证明,该方法对温度、孵育时间和底物浓度的刻意变化具有稳稳性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Quantitative Determination of Trypsin Inhibitory Activity in Complex Matrices
A quantitative assay using azocasein was developed to measure trypsin inhibitory activity in emulsions and other complex systems that are refractory to analysis. The method was tested for reproducibility on pure protein solutions as well as protein-containing material rich in fats and sugars, with special attention to emulsions. In the clean situation, the overall relative standard deviation was less than 6% while for the more complex systems it was less than 16%. The proce- dure proved robust against deliberate variations of temperature, incubation time and substrate concentration.
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