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

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Abstract

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.

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Authors and Affiliations

  1. Bioengineering Center of the Russian Academy of Sciences, Moscow, 117312, Russia

    D. V. Kurek, S. A. Lopatin & V. P. Varlamov

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  1. D. V. Kurek
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  2. S. A. Lopatin
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  3. V. P. Varlamov
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Correspondence to V. P. Varlamov.

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Original Russian Text © D.V. Kurek, S.A. Lopatin, V.P. Varlamov, 2009, published in Prikladnaya Biokhimiya i Mikrobiologiya, 2009, Vol. 45, No. 1, pp. 5–13.

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Kurek, D.V., Lopatin, S.A. & Varlamov, V.P. Prospects of application of the chitin-binding domains to isolation and purification of recombinant proteins by affinity chromatography. Appl Biochem Microbiol 45, 1–8 (2009). https://doi.org/10.1134/S0003683809010013

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  • DOI: https://doi.org/10.1134/S0003683809010013

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