Related Experiment Video
Updated: Feb 13, 2026

Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag
Published on: January 16, 2012
Chitosan/cellulose-based beads for the affinity purification of histidine-tagged proteins
Mingcong Shao1, Lili Xiu1, Haijiang Zhang2
1a College of Food Science and Biotechnology , Zhejiang Gongshang University , Hangzhou , P. R. China.
Abstract:
Chitosan/cellulose-based beads (CCBs) for the affinity purification of histidine-tagged proteins were prepared from chitosan/cellulose dissolved in ionic liquid as a solvent, and their structures were characterized by Fourier transform infrared spectroscopy, transmission electron microscopy, and thermogravimetric analysis. The affinity purification was used to separate hexahistidine-tagged (his-tagged) enhanced green fluorescent protein (EGFP) from Escherichia coli. The results showed that Zn2+-CCB exhibited more specific adsorption capacity toward the target protein compared with Ni2+-CCB and Cu2+-CCB. The maximum adsorption of EGFP was 1.84 mg/g of Zn2+-CCB, with 90% purity under the optimized conditions (ionic strength (1.0 M NaCl), pH (7.2) and imidazole concentration (500 mM)). In addition, a regeneration method for the sorbent was further developed by washing with ethylenediaminetetraacetic acid disodium and then reimmobilizing with metal ions. This technique is an alternative method for the purification of his-tagged proteins, making the process more economical, fast, stable, and large batch.
Related Concept Videos
Affinity and Avidity
Tagging and Fusion Proteins
Electron Affinity
Detergent Purification of Membrane Proteins
Protein Networks
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Cellulose and Pectic Polysaccharides
As a cell matures, its cell wall specializes according to its type. For example, the...

