Effect of antibody modifications on its biomolecular binding as determined by surface plasmon resonance

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• 作者：Sandeep Kumar Vashist ; ^{sandeep.vashist@yahoo.com} ; ^{sandeep.vashist@nus.edu.sg}
• 关键词：SPR ; Antibody modification ; Biomolecular binding ; Protein A ; Mouse IgG ; Goat anti-mouse IgG ; Atto 550 ; Atto 647 ; TRITC ; HRP ; Biotin
• 刊名：Analytical Biochemistry
• 出版年：2012
• 出版时间：1 February 2012
• 年：2012
• 卷：421
• 期：1
• 页码：336-338
• 全文大小：258 K

文摘

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.