protein self association - buffer effect
dk at no.email.thankstospam.net
Thu Sep 27 10:16:33 EST 2001
In article <126.96.36.199.0.20010927110036.00b23c20 at seita.roi.metla.fi>, francoise.martz at metla.fi (Francoise Martz) wrote:
>A plant protein was expressed in E.coli with a His tag and purified it
>using Ni-NTA spin column. On native PAGE, the protein appeared as oligomers
>in presence of tris or phosphate buffer, but appeared as monomer in
>presence of hepes or mops buffer (all at same pH).
>A similar (but weaker) self association was detected using plant crude
>extract (no His tag).
>Not a biochemist, I would be pleased to have any comment about the meaning=
>of these differences in oligomerization in different buffer conditions ?
Your protein interacts with Tris and phosphate ions in a way that
leads to self-accociation. But I guess you already know this :-)
Just one of those things... You can't know what it means unless you
study this intentionally.
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