Probing the functional heterogeneity of surface binding sites by analysis of experimental binding traces and the effect of mass transport limitation

J Svitel, H Boukari, D Van Ryk, RC Willson, P Schuck - Biophysical journal, 2007 - cell.com
Many techniques rely on the binding activity of surface-immobilized proteins, including
antibody-based affinity biosensors for the detection of analytes, immunoassays, protein …

Global analysis of a macromolecular interaction measured on BIAcore

LD Roden, DG Myszka - Biochemical and biophysical research …, 1996 - Elsevier
We demonstrate that the interaction between myoglobin and an immobilized anti-myoglobin
antibody measured on BIAcore 2000 can be described by a simple bimolecular reaction …

Interpreting complex binding kinetics from optical biosensors: a comparison of analysis by linearization, the integrated rate equation, and numerical integration

TA Morton, DG Myszka, IM Chaiken - Analytical biochemistry, 1995 - Elsevier
The binding kinetics recorded for many interactions using BIAcore and IAsys optical
biosensors do not fit a simple bimolecular interaction model (A+ B⇄ AB). Three methods of …

Evaluation of calibration-free concentration analysis provided by Biacore™ systems

E Pol, H Roos, F Markey, F Elwinger, A Shaw… - Analytical …, 2016 - Elsevier
Abstract Surface Plasmon Resonance biosensors measure the interaction between a
molecule in solution and its interaction partner attached to a sensor surface. Under certain …

Biomolecular interaction analysis: affinity biosensor technologies for functional analysis of proteins

M Malmqvist, R Karlsson - Current opinion in chemical biology, 1997 - Elsevier
The introduction of affinity-based biosensors has permitted label-free functional analysis of
biomolecular interactions in real time. A variety of methods are now based on BIACORE® …

The binding of antigen by immobilized antibody: Influence of a variable adsorption rate coefficient on external diffusion limited kinetics

A Sadana, D Sii - Journal of colloid and interface science, 1992 - Elsevier
The influence of reaction-order and external mass-transfer limitations on the binding kinetics
of antigen in solution to antibody covalently attached to a cylindrical fiber-optic biosensor is …

Visualizing two‐component protein diffusion in porous adsorbents by confocal scanning laser microscopy

T Linden, A Ljunglöf, MR Kula… - Biotechnology and …, 1999 - Wiley Online Library
The use of confocal scanning laser microscopy (CSLM) has recently been described for the
visualization of intraparticle protein profiles during single‐protein finite bath uptake …

A quantitative assessment of heterogeneity for surface-immobilized proteins

RA Vijayendran, DE Leckband - Analytical Chemistry, 2001 - ACS Publications
Many biotechnological applications use protein receptors immobilized on solid supports.
Although, in solution, these receptors display homogeneous binding affinities and …

Ligand loading at the surface of an optical biosensor and its effect upon the kinetics of protein–protein interactions

PR Edwards, PA Lowe… - Journal of Molecular …, 1997 - Wiley Online Library
Optical biosensors are finding increasing use in the determination of kinetic and equilibrium
constants for a variety of biomolecular interactions. Usually these biosensors require one …

Benefits and limitations of porous substrates as biosensors for protein adsorption

TD Lazzara, I Mey, C Steinem, A Janshoff - Analytical chemistry, 2011 - ACS Publications
Porous substrates have gained widespread interest for biosensor applications based on
molecular recognition. Thus, there is a great demand to systematically investigate the …