Abstract
To circumvent the difficulties encountered in conventional affinity chromatography, novel affinity-based protein purification processes using reversible protein-ligand interactions have been developed. Depending on the physical means of isolating the ligand-ligate complex, the processes can be categorized as affinity precipitation, affinity cross-flow filtration, or affinity partition. This report reviews the current status of such purification techniques.
| Original language | English |
|---|---|
| Pages (from-to) | 199-209 |
| Number of pages | 11 |
| Journal | Journal of Fermentation and Bioengineering |
| Volume | 70 |
| Issue number | 3 |
| DOIs | |
| State | Published - 1990 |
| Externally published | Yes |