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首页> 外文期刊>Journal of Biotechnology >Refolding of hexameric porcine leucine aminopeptidase using a cationic detergent and dextrin-10 as artificial chaperones
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Refolding of hexameric porcine leucine aminopeptidase using a cationic detergent and dextrin-10 as artificial chaperones

机译：使用阳离子去污剂和糊精-10作为人工伴侣，重整六聚体猪亮氨酸氨肽酶

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The application of artificial chaperones in biotechnology has been inspired by the mechanism of molecular chaperones like GroEL/GroES. It involves addition of a capturing detergent during dilution of the chaotropic reagent, that prevents protein aggregation, and finally, addition of a oligosaccharide that removes the detergent allowing the protein to refold. Here, guanidinium hydrochloride-denatured hexameric leucine aminopeptidase is shown to be efficiently refolded by using the cationic detergent cetyltrimethylammonium bromide and the linear polysaccharide dextrin-10 as artificial chaperones. The effect of these additives and the time dependence on the recovery of total enzymatic activity, kinetic parameters (K sub(M), k sub(c) sub(a) sub(t)), intrinsic steady-state tryptophan fluorescence and oligomeric structure is presented. The method described is very promising since 92% of fully active and correct folded LAP could be produced. Moreover, we showed that the stripping process is relatively slow, it allows the protein to refold almost entirely to its native state. electrophoresis
机译：人工分子伴侣在生物技术中的应用受到分子分子伴侣如GroEL / GroES机理的启发。它涉及在离液剂稀释期间添加捕获性去污剂，以防止蛋白质聚集，最后，添加寡糖以去除去污剂，使蛋白质重新折叠。在此，显示出通过使用阳离子去污剂十六烷基三甲基溴化铵和线性多糖糊精-10作为人工伴侣，盐酸胍变性的六聚亮氨酸氨基肽酶被有效地重折叠。这些添加剂的影响和时间依赖性对总酶活性，动力学参数（K sub（M），k sub（c）sub（a）sub（t）），固有稳态色氨酸荧光和低聚结构的恢复被表达。所描述的方法非常有前景，因为可以产生92％的完全活性和正确折叠的LAP。此外，我们证明了剥离过程相对较慢，它使蛋白质几乎可以完全折叠成其天然状态。电泳

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