In article <199603081023.CAA00509 at net.bio.net>
spagnol at GALACTICA.IT (Giorgio Spagnol) writes:
>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
Have you concidered that your "contaminants" could be a degradation product of
the glycoprotein you are immunoprecipitating? Also, glycoproteins may or may
not be glycosylated at each of their potential glycosylation sites. The size
differences may be due, in part, to differential glycosylation. Just a
thought.
Paula
U. of Louisville (KY)
>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.
>Cordially,
>Giorgio Spagnol
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