Determination of the PSMA affinity was performed by saturation binding assays using PC-3 PIP cells and different concentrations of nat/44Sc-, nat/68Ga-PSMA-6178Ga-PSMA-617, or nat/68Ga-PSMA-11 nat/68Ga-PSMA-11 nat/68Ga-PSMA-11.
The binding affinity tests were performed using a LigandTracer Yellow instrument provided by Ridgeview Instruments AB.
Linear correlations between the predicted binding scores and the experimentally measured binding affinities were observed.
TR-FRET-binding affinity assays were performed for BCL-2, BCL-XL, and MCL-1 in 4.52 mM monobasic potassium phosphate, 15.48 mM dibasic potassium phosphate, 1 mM sodium EDTA, 0.05% Pluronic F-68 detergent, 50 mM sodium chloride, and 1 mM DTT (pH 7.5) as described previously for BCL-XL.
While previous work to successfully achieve physiological binding affinities has been performed by employing site directed mutagenesis approaches, herein we undertake a different strategy, namely, truncation of the original protein to achieve the same goal.
To evaluate if the 52+2 Cys mutation influences the binding of the hapten into its binding pockets, affinity measurements were performed.
To study the effects of these modulators on the binding affinity of flurbiprofen, spectral binding studies were performed.
GR binding affinity assay was performed at Cerep Inc. (Celle l'Evescault, France), according to an established method [ 26].
To explore this possibility, binding affinity assay was performed to test the interaction between ECRG4 and ECRG1 proteins.
However, it needs to be noted that different methods have been used to determine these affinities, and that the binding assays were performed under different conditions that furthermore differ from those in planta during the interaction with the pathogen.
