[Protein-analysis] Disulphide bridges creation.

botulina at poczta.onet.pl botulina at poczta.onet.pl
Mon Nov 14 05:26:40 EST 2005

I have a protein which is suspected of creating homodimers, trimers and
so on when particular cysteines are forming intramolecular disulphide
bridge. The protein that I have after expression and purification
consists of mono- dim- and trimers. When I reduce the protein by DTT,
what I see are only monomers. When I purify the protein then on
sephadex to get read of DTT, and the protein is kept in solution of 20
mM ammonium acetate pH 7.5 for several hours (I need this crazy
solution for the experimental techmique) I can observe again the dimers
and trimers. Is the disulphide bridge formation possible in this
environment or should I rather exlude this mechanism?

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