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Binding kinetics were then assessed using twofold serial dilutions of antibody at concentrations ranging from 500 to 0.08 nM in running buffer (PBS, pH 7.4, 0.005% (v/v), polysorbate 20 – filtered and degassed) at 25°C and a flow rate of 25 ml/min.

The identification and quantification of contributions to the binding kinetics is then straightforward: in the depletion rate plot, the intercept at the vanishing free xenon concentration represents the kinetic rate coefficient for xenon detachment from the host by dissociative processes while the slope is indicative of the kinetic rate coefficient for degenerate exchange reactions.

diVCA binding and dissociation kinetics were then analyzed during those periods at each tethered-Arp2/3 location, as described below.

The binding kinetics were analyzed by BIAevaluation software (Biacore) using a 1 1 Langmuir binding model.

The binding kinetics were analysed with the software BIAevaluation Version 4.1 using the steady state affinity.

Antibody binding kinetics were determined by standard procedures, and affinity constants were calculated (Biaffin GmbH, Kassel, Germany).

The 11B6 binding kinetics were analysed by surface plasmon resonance using a Biacore 2000 (Biacore AB; Uppsala, Sweden).

As with ficolin-A, the binding kinetics were complex.

To distinguish between the two schemes, ATP binding kinetics were simulated for different sets of concentrations.

Since traditional in vitro methods belong to dose-dependent assessments, binding kinetics is usually overlooked.

Since both traditional in vitro methods belong to dose-dependent assessments, ligand-receptor binding kinetics is usually overlooked.