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Prospects of application of the chitin-binding domains to isolation and purification of recombinant proteins by affinity chromatography

机译:甲壳素结合结构域在亲和色谱分离纯化重组蛋白中的应用前景

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摘要

Properties of substrate-binding domains, some parameters of affinity sorbents, and a number of other special features that were necessary to take into account during creation of chromatographic system for isolation and purification of proteins with incorporated chitin-binding domain were discussed in this review. This method was shown to be successfully used along with metal-chelate affinity chromatography. The metal-chelate affinity chromatography with the use of polyhistidine peptides as affinity labels is successfully applied to isolation, purification, and investigation of recombinant proteins. However, this system had some disadvantages. At present, scientists attracted more and more attention to substrate-binding domains, including those chitin-binding, because they had a number of advantages being used as affinity label. (PUBLICATION ABSTRACT)
机译:在这篇综述中讨论了底物结合域的性质,亲和吸附剂的一些参数以及在色谱系统创建过程中必须考虑的许多其他特殊特征,这些层析系统用于分离和纯化具有掺入几丁质结合域的蛋白质。已证明该方法已成功与金属螯合亲和色谱法一起使用。使用多组氨酸肽作为亲和标记物的金属螯合亲和色谱法已成功应用于重组蛋白的分离,纯化和研究。但是,该系统具有一些缺点。目前,科学家们越来越关注底物结合域,包括那些几丁质结合域,因为它们具有许多亲和标记的优势。 (出版物摘要)

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