Protein purification by affinity chromatography
1. Chromatography is defined as a biophysical technique employed for the separation, identification and purification of the individual components of a mixture, based on their differential properties, for qualitative and quantitative analysis. It can be used to separate a mixture of _______.
2. The chromatographic technique that exploits the property of highly specific binding between an immobilized ligand and a only single component of the analyte mixture, is termed as _______.
3. Affinity chromatography can be used to purify biomolecules using corresponding resins to which they specifically bind. Find the correct match of the resin and its eluate
4. Affinity chromatography is used to isolate biomolecules bound to one another and study their interaction using a ligand that specifically binds to one of the biomolecules in the complex. This technique is termed as _______.
5. To elute the desired analyte, it needs to be freed from the analyte-ligand complex. This is achieved by adding in a competitor that binds more strongly with the ligand. This method is called specific elution. Non-specific elution is achieved using _______.
6. In immobilized metal affinity chromatography (IMAC), the commonly used metal is _______.
7. Ni-NTA chromatography is a common type of IMAC commonly used in FPLC for the purification of proteins with a recombinant hexahistidine tag. What is the principle behind the affinity?
8. FPLC is a type of affinity chromatographic technique that uses Ni-NTA IMAC for the purification of proteins. FPLC stands for _______.
9. In FPLC, the flow rate of the liquid mobile phase through the column can be controlled
10. FPLC finds application in _______.