Can anyone help me with this problem? I have a pure microbial protein
which when run on an SDS non-reduced (ie no mercaptoethanol) PAGE gel
runs at approximately 50 KDa. When the same protein is run under
SDS-reduced conditions two subunits appear- one running at approx 40 KDa
and the other at approx 60 KDa.
It was my understanding that the two subunits should add up to be the
same size as the protein run under SDS-non reduced conditons. But this
isn't happening. Does anyone know why?
