Biointeraction analysis by high-performance affinity chromatography: Kinetic studies of immobilized antibodies

Analytical methods for kinetic studies of biological interactions: A review

“…Other drugs (e.g., diazepam, imipramine, acetohexamide, tolbutamide, amitriptyline, quinidine, verapamil, amitriptyline, lidocaine, and nortriptyline) and binding agents (e.g., alpha 1 -acid glycoprotein) have also been studied with this method [142,143]. The peak decay method has further been employed to study the dissociation rates of various targets from immobilized antibodies during the selection of elution conditions for immunoaffinity chromatography [144]. In addition, this method has been used to characterize the elution kinetics of thyroxine from columns containing anti-thyroxine antibodies or aptamers, and the dissociation of IgG-class antibodies from immobilized protein G [145,146].…”

“…The peak decay method has been used with application buffers to examine several systems with weak-to-moderate affinities (i.e., K 1 < 10 6 M −1 ) [140–144]. It has also been used to study the elution conditions needed for systems with stronger binding (e.g., protein G, antibodies and aptamers) [145,146].…”

Recent advances and future trends in new materials for sample preparation

“…Immunosorbents are antibodies immobilized on a solid or gel support (e.g., silica or cellulose) and take advantage of highly-specific antigen-antibody interactions to afford molecular recognition, allowing good selectivity and low LODs [123]. They have been used for several applications (e.g., drugs, pesticides and PAHs) [124].…”

“…Nelson et al [123] developed supports that contained mAbs for 2,4-dichlorophenoxyacetic acid using high-performance affinity chromatography. The method was efficient for investigation of small mAbs, providing information about application, elution and regeneration kinetics of immobilized mAbs.…”

Measuring Binding Constants of His-Tagged Proteins Using Affinity Chromatography and Ni-NTA-Immobilized Enzymes

“…Frontal analysis affinity chromatography has previously been used to determine the binding constants of enzymes [3][4][5][6][7] as well as other affinity interactions including drug-protein binding constants [1,8] and antibody-antigen binding constants [9]. Multiple methods of immobilization exist and include both covalent and noncovalent methods [3].…”