5. MCQ; a. Affinity chromatography is a biochemical method that involves specifi

Question

5. MCQ; a. Affinity chromatography is a biochemical method that involves specific interactions of molecules and immobilized ligand. This method takes an advantage of: i. Protein's charge ii. Protein's mass iii. Protein's structure iv. All of the above b. Purification of an antigen using specific antibody is an example of i. Ion-exchange chromatography ii. Gel filtration iii. Affinity chromatography iv. Salting out c. Affinity chromatography involves all following bonds except: i. Hydrogen bonds ii. Hvdrophobic interactions iii. Ionic bonds iv. Covalent bonds d. Affinity chromatography can purify all following proteins except: i. Glucose oxidase 11. Insulin iii. IgG iv. BSA e. The proteolytic cleavage site is often introduced between GST and the protein of interest to: i. Ensure better separation from the column ii. Help protein to fold properly iii. Remove the tag after purification iv. Keep the structural integrity of the protein

Explanation / Answer

any of the chromatography is based on charge of protein, mass of the protein and structure of the protein. Hence the answer is,

iv. all of the above.

iii. affinity chromatography. Specific antibody or legand is selected for purification of antigen in affinity chromatography.

Hydrophobic interaction chromatography is based on interaction of protein with hydrophobic adsorbents molecules which depends on salt concentration of solution. This interaction is not possible in affinity chromatography hence the answer is,

II. hydrophobic interaction

iv. bovine serum albumin. Bovine albumin consist of more than 50% of oart of serum hence it is important to remove albumin first before separation in affinity chromatography.

The protiolytic cleavage site present between protein and GST iii remove the tag after purification of protein. Because after purification this GST tag is no longer required.

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