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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Jack bean urease (EC 3.5.1.5) aggregation monitored by dynamic and static light scattering
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Jack bean urease (EC 3.5.1.5) aggregation monitored by dynamic and static light scattering

机译:通过动态和静态光散射监控波豆脲酶(EC 3.5.1.5)聚集

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摘要

Aggregation of jack bean urease (JBU) is involved in many alterations of its biological properties, notably the ureolytic and entomotoxic activities. In order to investigate this phenomenon, protein aggregates were characterized by dynamic (DLS) and static light scattering (SLS) spectroscopies through determination of apparent hydrodynamic radii, the average molecular masses, radii of gyration and second virial coefficients. No effect of disulfide reducing agents on protein association was observed contrasting with previous reports implicating their function in the prevention of JBU aggregation. The influence of freeze-thawing cycles on protein aggregation was also investigated. Our results showed that after freeze-thawing cycles the native form of JBU with apparent hydrodynamic radius of 7 nm and radius of gyration of 12 nm is replaced by high-order oligomers and this aggregation is not reverted neither by dithiothreitol (DTT) treatment nor by high concentration of salts. Altogether the data help to understand the complex behavior of JBU in solution and may correlate with the diversity of biological properties of this enzyme. (C) 2004 Elsevier B.V. All rights reserved.
机译:杰克豆脲酶(JBU)的聚集涉及其生物学特性的许多变化,特别是尿素分解和昆虫毒性活性。为了研究这种现象,通过测定表观流体动力学半径,平均分子量,回转半径和第二病毒系数,通过动态(DLS)和静态光散射(SLS)光谱对蛋白质聚集体进行表征。与以前的报道暗示其在预防JBU聚集中的功能相反,未观察到二硫化物还原剂对蛋白质缔合的影响。还研究了冻融循环对蛋白质聚集的影响。我们的结果显示,在冻融循环后,JBU的天然形式的表观流体动力学半径为7 nm,回转半径为12 nm,被高阶低聚物取代,并且这种聚集作用既不会被二硫苏糖醇(DTT)处理也不会被还原。高浓度的盐。总而言之,数据有助于了解JBU在溶液中的复杂行为,并且可能与该酶的生物学特性相关。 (C)2004 Elsevier B.V.保留所有权利。

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