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Online substrate cleavage was monitored by measuring binding of mAb10F12 to a SNAP-25 neo-epitope.
Joshi et al. [5] tried to address this problem by measuring binding of phospholipidosis-inducing drugs to L-α-dipalmitoyl phosphatidylcholine vesicles.
To prove our hypothesis, we used two-dimensional heteronuclear correlation NMR spectroscopy, which is suitable for measuring binding of a given ligand to a protein.
This phenomenon works in our favor, as it means that vanishingly little MANT-ATP will be hydrolyzed over the time-scale of our experiments, ensuring that we are measuring binding of an ATP and not an ADP mimetic.
The immunoreactivity was determined by measuring binding of Zr-cU36, Zr-cetuximab, or Zr-rituximab (10,000 cpm/ml) to a serial dilution of 0.2% glutaraldehyde-fixed 11B cells or 2% paraformaldehyde-fixed A431, or Ramos cells, respectively, essentially as described by Lindmo et al. [ 19].
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To determine whether cells that are relatively insensitive to AprA have an observable defect in the ability of rAprA to bind to this receptor, we measured binding of rAprA to cells.
The K472E/R473E mutant Cul1 was then used to measure binding of CAND1 by coimmunoprecipitation.
We measured binding of CquiOBP1 to a few compounds known/inferred to be mosquito attractants.
Figure 1 is a schematic representation of the production of the 32P-labeled peptides and the experimental design of assays to measure binding of peptides to cell lines.
Isothermal titration calorimetry (ITC) was used to measure binding of the individual human or mouse NOXO1 SH3andnd SH3B domains to the p22phox cytoplasmic domain.
A sandwich ELISA was used to measure binding of peptide-free or peptide-loaded DR1 to LB3.1 and MEM264 as previously described [22].
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