[Prospects of application of the chitin-binding domains to isolation and purification of recombinant proteins by affinity chromatography: a review]

Prikl Biokhim Mikrobiol. 2009 Jan-Feb;45(1):5-13.
[Article in Russian]

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Chitinases / chemistry
  • Chitinases / metabolism
  • Chromatography, Affinity
  • Cross-Linking Reagents / chemistry
  • Glutaral / chemistry
  • Histidine / metabolism*
  • Protein Binding
  • Protein Structure, Tertiary
  • Recombinant Proteins / isolation & purification*
  • Recombinant Proteins / metabolism

Substances

  • Cross-Linking Reagents
  • Recombinant Proteins
  • polyhistidine
  • Histidine
  • Chitinases
  • Glutaral