In article <32CDEA59.735A at jcu.edu.au>, lachlan harris
<lachlan.harris at jcu.edu.au> wrote:
--> 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?
a quick guess ... couldn't it be heterogeneous conformations ...
for example, OmpA of E coli runs on gels as two forms, based on
"heat modfiability" ... i.e., whether or not the OmpA has been
boiled or not prior to loading on the gel... just a thought
good luck
-d
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