How did you arrive at the 10KDa difference - is it through the observation
of the gel or via something more accurate e.g. MS ? If you use MS then you
should be able to find out where exactly the truncation is occurring, if it
is indeed a truncation and not something more exotic.
In bacteria, protein splicing events are not frequent - most likely your
truncation is due to proteolysis, either by protease(s) or via chemical
means such as the DP acidic/heat cleavage.
If you would be willing to share more details, perhaps we can arrive to more
detailed conclusions :)
A.G.E.
"Tom La" <tom_la at central.murdoch.edu.au> wrote in message
news:3E4DFD5B.5040309 at central.murdoch.edu.au...
> Hi guys,
> I am working on a bacterial protein in which the deduced MW (from gene
> sequence) is about 10 kDa larger than the native extracted protein. I am
> sure that the sequence is correct and that the deduced and native
> proteins are the same. Can anyone suggest a possible explanation for the
> difference in size? Thanks in advance.
> Regards,
> Tom
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