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The apparent binding constant has been obtained.
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The values of binding constant have been determined to be 4.1 × 105 M−1 and 4.8 × 105 M−1; and 5.2 × 105 M−1 and 5.6 × 105 M−1 for ETO and ETO cation free radical in phosphate buffer solutions of pH 4.5 and 7.4; respectively.
Binding stoichiometry and binding constants have been investigated to determine the ratio and relative stability of Fe3+ complexes.
Fluorescent enhancement has been explained on the basis of photo-induced electron transfer (PET) mechanism and apparent binding constants have been deduced.
The binding constants have been estimated to be K ~ 10 M−1 for all the temperatures used.
Her only constant has been change.
The constant has been Brett Favre.
Given that many inhibitors have been studied and for many of them binding affinity constants have been calculated, it is beneficial to analyze the chemical landscape of these families of inhibitors and correlate these inhibition constants with molecular structure descriptors.
Equilibrium constants have been determined for Hg2+ binding with the enzyme or the enzyme-substrate complexes (Ki =0.012 μM).
The apparent binding constants (Kapp) has been obtained 3.9 and 10.9 × 104 M−1 at lower concentration range and 1.03 and 1.59 × 104 M−1 at higher concentration range for complexes (1) and (2), respectively.
In addition to the B2 Ab binding experiments here, FcγR binding of G1Δab and G1Δac constant regions has been compared in the context of Fog-1 and CAMPATH variable regions without the null allotype mutations 1, 3, 4. The hierarchy of binding to each receptor was retained whatever the setting of the mutations.
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