title: Effect of antibody modifications on its biomolecular binding as determined by surface plasmon resonance.
abstract: A surface plasmon resonance (SPR)-based procedure was developed to determine the effect of antibody modifications on its biomolecular binding behavior. Mouse immunoglobulin G (IgG) was immobilized on a protein A-functionalized gold-coated SPR chip. Goat anti-mouse IgG and its various commercially available modifications (i.e., conjugated with atto 550, atto 647, tetramethylrhodamine isothiocyanate [TRITC], horseradish peroxidase [HRP], or biotin) were employed in exactly the same concentration for the detection of mouse IgG. The various modifications of goat anti-mouse IgG decreased its biomolecular binding to mouse IgG in the order of unmodified>HRP-labeled>atto 550-labeled>biotinylated>TRITC-labeled>atto 647-labeled.
authors.affiliation: Centre for Bioanalytical Sciences, National Centre for Sensor Research, Dublin City University, Dublin 9, Ireland. sandeep.vashist@yahoo.com
authors.forename: Sandeep Kumar
authors.initials: SK
authors.lastname: Vashist
mesh_terms: D000818:Animals; D000888:Antibodies, Anti-Idiotypic / Q000737:chemistry; D055910:Antibodies, Immobilized / Q000737:chemistry; D001666:Binding Sites, Antibody; D001710:Biotin; D006041:Goats; D006576:Heterocyclic Compounds, 4 or More Rings; D006735:Horseradish Peroxidase; D007074:Immunoglobulin G / Q000737:chemistry; D051379:Mice; D012235:Rhodamines; D020349:Surface Plasmon Resonance / Q000379:methods*
chemical_list: D000888:Antibodies, Anti-Idiotypic; D055910:Antibodies, Immobilized; C521550:Atto590; D006576:Heterocyclic Compounds, 4 or More Rings; D007074:Immunoglobulin G; D012235:Rhodamines; C009434:tetramethylrhodamine isothiocyanate; D001710:Biotin; D006735:Horseradish Peroxidase