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Metal binding is monitored by the appearance of a new LMCT band at 238 nm.
Successful binding is monitored by measuring the energy transfer between the Tb energy donor and the fluorescently labeled leptin energy acceptor.
The binding is monitored by following the change in the square wave voltammetry (SWV) reduction peak signal of ferrocyanide/ferricyanide redox couple due to the removal of the negatively charged aptamers from the surface upon protein binding.
Unspecific binding is monitored by competition with an oligonucleotide containing the consensus PPAR γ response element sequence, according to the manufacturer's protocol.
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Binding was monitored by the colorimetric conversion of nitrocerfin by a β-lactamase fusion to DCC.
The protein binding was monitored by FET and direct current (dc) measurements.
SA binding was monitored by EMSA assay after treatment with urea and 0.5% SDS, which disrupts binary and ternary RT complexes but not the SA-biotin linkage (25).
The extent of cell cell binding was monitored by measuring the disappearance of single cells using the Coulter Counter Z1.
The binding was monitored by OD492 measurements after reaction with the peroxidase-conjugated goat anti-mouse IgG (Sigma).
After washing, binding was monitored by hybridizing Alexa Fluor 647-conjugated secondary antibody and quantifying fluorescence on a flow cytometer.
Binding was monitored by fluorescence intensity changes of FAM-RNA upon addition of protein [FAM does not alter RNA binding affinity (see Materials and Methods)].
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