A homodimeric protein was found to migrate through SDS polyacrilamide gel electrophoresis (SDS-PAGE) with a mobility that matched that of a 45-kDa standard. What change in the experiment would increase the chances of observing the mobility expected for the 22.5-kDa monomer? A. Increasing the gel running timeB. Adding a reducing agentC. Using a higher voltageD. Removing the SDS

Question

Ray Black

Physics

31 March, 19:55

A homodimeric protein was found to migrate through SDS polyacrilamide gel electrophoresis (SDS-PAGE) with a mobility that matched that of a 45-kDa standard. What change in the experiment would increase the chances of observing the mobility expected for the 22.5-kDa monomer? A. Increasing the gel running timeB. Adding a reducing agentC. Using a higher voltageD. Removing the SDS

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Kaufman · Answer 1

Adding a reducing agent

Explanation:

Homodimeric proteins are formed by non-covalent interactions between two identical proteins (monomers).

Some of these intermolecular interactions are mediated by disulphide bonds which can be broken by a reducing agent like beta-mercaptoethanol (2-ME).

By adding the reducing agent to the gel, it is probable that the dimer is broken and the band observed will correspond to the two identical 22.5-kDa monomers.