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Critical analysis of lysozyme refolding kinetics

机译：溶菌酶复性动力学的临界分析

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The kinetics of lysozyme refolding and aggregation is studied using an existing competing first-and third-order reaction scheme.The existing mode loverestimates yield at high refolding concenratios (>1 mg/mL),thuslimiting its sue for reactor designat industrially relevant refolding concentrations.This study demonstrtes that a pathway exists for the incorporation of refolded native protein into aggregates.Specifically,native lysozyme labeled with fluorescein isothiocyanate was added to the refolding buffer prior to dilution refolding of denatured and reduced lysozyme.Aggregates collected from these experiments showed significant fluorescence,indicating that labeled lysozyme had been incorporated into the aggregates during refolding.Although the precise pathway of incorporation has not been elucidated,it is clear from this work that the existing model for lysozyme refolding is not globally applicable.In particular,previous work has analytically demonstrated that neglect of a pathway from native to aggregate canresult in the design of a grossly suboptimal reactor strategy.This study demonstrates that such a pathway can exist experimentally and emphasizes the need tocritically assess refolding kinetic models before their use in reactor design equations.
机译：使用现有的竞争性一阶和三阶反应方案研究了溶菌酶重整和聚集的动力学。现有模式在高重折叠浓度（> 1 mg / mL）时重估了收率，因此限制了其在工业相关重整浓度下用于反应器设计的要求。这项研究表明存在一条将重新折叠的天然蛋白整合到聚集体中的途径。具体来说，在变性和还原的溶菌酶稀释重折叠之前，将标记有异硫氰酸荧光素的天然溶菌酶添加到重折叠缓冲液中。这表明标记的溶菌酶已经在重折叠过程中被整合到聚集体中。虽然尚未阐明掺入的确切途径，但是从这项工作中可以清楚地看到，现有的溶菌酶重折叠模型并不适用于全球。特别是，先前的工作已经通过分析证明忽略了来自这项研究表明，这种途径可以实验性地存在，并强调需要在将重折叠动力学模型用于反应堆设计方程之前对其进行严格评估。

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