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Generally, two types of binding kinetics could be observed in our experiments.
To explore whether the different binding kinetics could be affecting agonism, a time-course experiment was performed with FasL, E09 and the variant antibodies, measuring the rate of caspase 3/7 activation in Jurkat cells.
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If PBA is directly binding to the channel, the slowed kinetics could be explained by a cytoplasmic or buried binding site.
In addition, secondary plot data have indicated that some Grxs may have infinite Michaelis Menten binding constants [ 16] implying that mass action kinetics could be used to describe the Grx redox cycle [ 20].
Generalized mass-action kinetics could be helpful for this purpose.
Hence, the kinetics of lectin binding could be influenced by the diffusion of the lectin within the chamber and result in an increase of lectin binding over a longer time period.
A characteristic binding motif could be deduced.
In this respect, side-binding proteins could be thought of as allosteric regulators of actin filament kinetics.
This binding could be inhibited by heparin.
An alternate explanation for the bimodal peak pattern could be slow binding kinetics of peptide 2 (slow kon), a phenomenon that has been observed previously.
Due to noticeable signal noise, colloid-induced signal deconvolution using binding kinetics appeared to be inaccurate.
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