Publication details
Afinitní ultrafiltrace bílkovin
| Title in English | Affinity Ultrafiltration of Proteins |
|---|---|
| Authors | |
| Year of publication | 2000 |
| Type | Article in Periodical |
| Magazine / Source | Chemické Listy |
| MU Faculty or unit | |
| Citation | |
| Field | Biochemistry |
| Keywords | Affinity Ultrafiltration |
| Description | Affinity ultrafiltration combines high volume processing capability of membrane filtration with high selectivity that can be achieved in affinity methods of protein purification This technique works on the principle that when a protein to be purified is free in solution, it passes through the ultrafiltration membrane., whereas when it is bound to a macromolecular affinity ligand placed on one side of the membrane, it is restricted to that side of the membrane. Compounds which do not bind the ligand pass freely through the membrane and are thus separated from the protein-ligand complex. After all the undesired components have been removed, the protein is desorbed from the ligand by the addition of an appropriate dissociating medium and is then recovered in the filtrate. The paper describes basic principles and characteristics of the method. In addition some applications of affinity ultrafiltration for protein purification are given. |
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