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A multimeric proteins when run on an SDS gel showed 2 bands at 20 kDa and 40 kDa. However, when the protein was run on a native gel, showed a single
A multimeric proteins when run on an SDS gel showed 2 bands at 20 kDa and 40 kDa. However, when the protein was run on a native gel, showed a single band at 120 kDa. The native from of the protein would be
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In SDS PAGE, SDS (denaturing agent) cleaves the 120kd multimeric protein into four subunits 2 X 20 kd + 2 X 40kd. However, Native PAGE doesn't separate the subunits of proteins, so it gives 120KD as total weight. Here the four subunits have different weights. So the native form of protein would be Heterotetramer.