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Pure IgG antibody was run on an SDS-PAGE under reducing condition. How many bands would you see after staining with Coomassie blue?
- a)4
- b)2
- c)1
- d)6
Correct answer is option 'B'. Can you explain this answer?
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Pure IgG antibody was run on an SDS-PAGE under reducing condition. How...
Answer:
Under reducing condition, pure IgG antibody will be separated into two heavy chains and two light chains, resulting in two bands on SDS-PAGE.
Explanation:
SDS-PAGE is a technique used to separate proteins based on their size. SDS (sodium dodecyl sulfate) is an anionic detergent that denatures the proteins and gives them a uniform negative charge relative to their size. When loaded onto a polyacrylamide gel and subjected to an electric field, the proteins migrate through the gel according to their size.
In reducing conditions, a reducing agent like beta-mercaptoethanol or dithiothreitol (DTT) is added to break the disulfide bonds that hold the protein together. This results in the separation of the IgG antibody into its constituent heavy and light chains.
Coomassie blue is a dye that binds to proteins and allows them to be visualized on the gel. It stains all proteins with equal affinity, regardless of their function or structure.
Therefore, under reducing conditions, we would expect to see two bands on the SDS-PAGE gel stained with Coomassie blue, corresponding to the two heavy chains and two light chains of the IgG antibody.
Thus, the correct answer is option B, 2 bands.
Under reducing condition, pure IgG antibody will be separated into two heavy chains and two light chains, resulting in two bands on SDS-PAGE.
Explanation:
SDS-PAGE is a technique used to separate proteins based on their size. SDS (sodium dodecyl sulfate) is an anionic detergent that denatures the proteins and gives them a uniform negative charge relative to their size. When loaded onto a polyacrylamide gel and subjected to an electric field, the proteins migrate through the gel according to their size.
In reducing conditions, a reducing agent like beta-mercaptoethanol or dithiothreitol (DTT) is added to break the disulfide bonds that hold the protein together. This results in the separation of the IgG antibody into its constituent heavy and light chains.
Coomassie blue is a dye that binds to proteins and allows them to be visualized on the gel. It stains all proteins with equal affinity, regardless of their function or structure.
Therefore, under reducing conditions, we would expect to see two bands on the SDS-PAGE gel stained with Coomassie blue, corresponding to the two heavy chains and two light chains of the IgG antibody.
Thus, the correct answer is option B, 2 bands.
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Pure IgG antibody was run on an SDS-PAGE under reducing condition. How many bands would you see after staining with Coomassie blue?a)4b)2c)1d)6Correct answer is option 'B'. Can you explain this answer?
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