The effect of adsorption on the antigen binding by IgG and its F(ab')2 fragments.
作者： Jos Buijs , David D. White , Willem Norde
DOI: 10.1016/S0927-7765(96)01327-6
关键词: Ionic strength 、 Immunoassay 、 Charge density 、 Chemistry 、 Stereochemistry 、 Sorbent 、 Electrostatics 、 Antigen 、 Adsorption 、 Molecule 、 Crystallography
摘要: Abstract The adsorption process of two monoclonal IgGs and their F(ab′)2 fragments is related to the efficiency with which these adsorbed proteins bind antigens. Adsorption antigen binding experiments are performed under various conditions hydrophobicity sorbent surface, pH ionic strength. immobilization followed in time using optical technique reflectometry. From previous results it has been inferred that Fc part an IgG molecule structurally less stable than part. This lower structural stability promotes molecules parts directing Fab towards solution. Indeed, found ratios higher at affinity for surface relatively low. Furthermore, observed orientation uneven charge distribution can be strongly influenced by electrostatic interactions. a total absence immunological activity when electrostatically attracted surface.
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