why

Frank Fuerst fant.1 at gmx.net
Wed Feb 16 07:29:52 EST 2000


> Zhang Bo wrote:
> 
> Dear Netters,
> We have expressed a recombinant protein in E.Coli, and we get the
> purified product. But when we determined its molecular weight by
> MS(mass spectrometry), it has 500 dalton more than expected. Then we
> sequenced the product, its N-terminal sequence and the last two
> amino acid are O.K. So I wonder why?


Even in E.coli, some proteins get modified after translation. I'm
quite sure that there is some glycosylation, but there might be other
modifications, too.
 
Frank
-- 
Frank Fuerst, PhD-Student
Department of physical biochemistry
Potsdam Unversity, Germany




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