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Non-specific adsorption of serum proteins to Eupergit C (EC) and agarose during the process of immunoaffinity chromatography often leads to contamination of the specifically eluted antigens to be purified. This effect was studied by application of serum samples to a beta-mercaptoethanol-blocked EC (EC-beta ME) column followed by analysis of proteins eluted with various elution buffers. Inclusion of polyethylene glycol (PEG 400 or 1500) in the loading buffer reduced the non-specific adsorption of proteins to EC but had an adverse effect on agarose. Covalent attachment of amino-PEG to EC and to epoxy-activated Sepharose mimicked the effect of PEG in solution with EC and resulted in a marked reduction in non-specific adsorption of serum proteins. Inclusion of PEG in the loading buffer during immunopurification of a serum protein (immunoglobulin G) or seminal plasma protein (human decidua protein hDP71) resulted in a marked improvement in the purity of these proteins eluted from the respective columns by ammonium acetate (pH 10).
G Fleminger, and
B Solomon, and
T Wolf, and
E Hadas
February 2011,
Biomacromolecules,
G Fleminger, and
B Solomon, and
T Wolf, and
E Hadas
February 2016,
ACS applied materials & interfaces,
G Fleminger, and
B Solomon, and
T Wolf, and
E Hadas
January 2006,
Bioconjugate chemistry,
G Fleminger, and
B Solomon, and
T Wolf, and
E Hadas
May 2016,
Materials science & engineering. C, Materials for biological applications,
G Fleminger, and
B Solomon, and
T Wolf, and
E Hadas
January 1999,
Transfusion,
G Fleminger, and
B Solomon, and
T Wolf, and
E Hadas
January 1985,
Thrombosis research,
G Fleminger, and
B Solomon, and
T Wolf, and
E Hadas
January 1996,
Electrophoresis,
G Fleminger, and
B Solomon, and
T Wolf, and
E Hadas
June 1976,
Thrombosis research,
G Fleminger, and
B Solomon, and
T Wolf, and
E Hadas
January 1999,
Bioconjugate chemistry,
G Fleminger, and
B Solomon, and
T Wolf, and
E Hadas
December 2014,
Macromolecular bioscience,
