If you have a native gel that shows a single 60 kd band and then do an SDS PAGE
ID: 186877 • Letter: I
Question
If you have a native gel that shows a single 60 kd band and then do an SDS PAGE gel on the same sample. The SDS page shows a single line that is 15 Kd what can we assume about this protein.
A protein was purified to a homogenous sample. The protein sample was then subjected to both Native gel and SDS-PAGE gel analysis, the results are shown below. Using the results of both gels, discuss any tertiary and quaternary structure of the protein (include MW). Native Gel SDS-PAGE Gel Sample 75D 50 D_ 50 kDI-- 20BD 20kD| 10kD|- 5 kD_Explanation / Answer
The native page does not denature the protein. Thus we can interpret from the gel that the molecular weight of the protein in its quarternary structure is around 60 kD.
The SDS-Page however causes denaturation of proteins and DTT breaks the disulphide bridges. Thus we can interpret from the gel that the weight of the protein in its tertiary state is 30kD while that in the Primary state is around 15kD
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