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Affinity Chromatography Video Lecture | Crash Course for CSIR NET Life Sciences
FAQs on Affinity Chromatography Video Lecture - Crash Course for CSIR NET Life Sciences
| 1. What is affinity chromatography and how does it work? |  |
Ans. Affinity chromatography is a specialized technique used to separate and purify biomolecules based on specific interactions between a target molecule and a ligand that is immobilized on a solid support. The process involves passing a mixture through a column containing the immobilized ligand. The target molecules bind to the ligand while other components are washed away. The bound target can then be eluted using a solution that disrupts the interaction, allowing for its collection in a purified form.
| 2. What are the key applications of affinity chromatography in research and industry? | |
Ans. Affinity chromatography is widely used in various fields, including biochemistry, molecular biology, and pharmaceuticals. Key applications include the purification of proteins, antibodies, and nucleic acids, as well as the removal of contaminants from biological samples. It is also utilized in the production of vaccines and therapeutic proteins, where high purity is essential for efficacy and safety.
| 3. What are some advantages of using affinity chromatography compared to other chromatography methods? | |
Ans. Affinity chromatography offers several advantages, including high specificity and selectivity, which leads to enhanced purity of the target molecule. It also typically requires fewer purification steps, saving time and resources. Additionally, the ability to utilize specific interactions allows for the purification of complex mixtures, which is particularly valuable in biochemical research and industrial applications.
| 4. What factors should be considered when selecting a ligand for affinity chromatography? | |
Ans. When selecting a ligand for affinity chromatography, several factors should be considered, including the nature of the target molecule, the strength and specificity of the interaction, and the conditions required for binding and elution. The ligand should have a high affinity for the target molecule while allowing for easy elution. Compatibility with the buffer system and the stability of the ligand under operational conditions are also crucial for successful separation.
| 5. How can the efficiency of affinity chromatography be optimized? | |
Ans. The efficiency of affinity chromatography can be optimized by adjusting various parameters such as flow rate, buffer composition, pH, and temperature. It is also important to ensure that the ligand density is appropriate for the target molecule and that the column is properly equilibrated before use. Regular monitoring of the binding and elution conditions can help identify the optimal parameters for specific applications, leading to improved yields and purity of the target molecule.
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Sep 28, 2025
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