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A protein was run under native conditions in a gel filtration column and was calculated to be of 120 kDa in size. The molecular weight of the protein in SDS-PAGE was found to be 30 kDa. The oligomeric status of the protein is

Question

A protein was run under native conditions in a gel filtration column and was calculated to be of 120 kDa in size. The molecular weight of the protein in SDS-PAGE was found to be 30 kDa. The oligomeric status of the protein is

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Solution

The oligomeric status of the protein can be determined by comparing the molecular weight of the protein under native conditions and denaturing conditions (SDS-PAGE).

Under native conditions, the protein was found to be 120 kDa, while under denaturing conditions (SDS-PAGE), it was found to be 30 kDa.

The denaturing conditions of SDS-PAGE break down the protein into its individual subunits. Therefore, the molecular weight found under these conditions (30 kDa) corresponds to the weight of a single subunit of the protein.

To find the oligomeric status of the protein, you divide the total molecular weight of the protein under native conditions by the molecular weight of a single subunit.

So, 120 kDa / 30 kDa = 4

Therefore, the protein is a tetramer, meaning it is composed of four subunits.

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