Salt-independent adsorption of human serum proteins on cyanocarbon gels.
Electron donor acceptor gels based on cyanocarbons have been tested for human serum protein adsorption in the absence of salt-promotion by water-structuring salt. This phenomenon was compared with a normal adsorption process in the presence of salt. The tricyanoaminopropene-divinyl sulfone-agarose displayed unusual protein adsorption properties as binding could occur both independently or dependently of the salt-promotion. The absence of hydrophobic or ionic character of the salt-independent interaction suggests an electron donor acceptor adsorption mechanism which is shown, for the first time, to occur independently of salt-promotion in aqueous solution. Study of the protein adsorption specificity showed similar protein selectivity for the fractions adsorbed in both conditions.
Berna
P P
PP
Biochemical Separation Centre, Uppsala University, Sweden.
Porath
J
J
D000327:Adsorption; D001798:Blood Proteins / Q000032:analysis*; D002847:Chromatography, Agarose; D015180:Electrophoresis, Gel, Two-Dimensional; D005782:Gels; D006801:Humans; D008024:Ligands; D009570:Nitriles; D015203:Reproducibility of Results; D012965:Sodium Chloride; D013431:Sulfates
D001798:Blood Proteins; D005782:Gels; D008024:Ligands; D009570:Nitriles; D013431:Sulfates; C012036:sodium sulfate; D012965:Sodium Chloride