Dear fellow netters,
When I precipitate a glycoprotein I'm studiyng with a monoclonal Ab
against the peptidic part, two contaminants of lower molecular weight
(It actually seems one, when I run nondenaturing gels) always
co-precipitate. Consider that the protein is precipitated after
extraction of integral membrane proteins with 1% Triton and eluted from
the antibody at high PH and exchanging triton with octylglucosyde,
always at physiologic pH.
If anybody could help me in get rid of this fastidious contaminant, I
would be very grateful.