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The corrected binding affinity of clozapine Kb was calculated using the Cheng-Prusoff equation [31]: Kb = IC50/(1+[agonIC50/EC50).
These data demonstrate that the sequence between restriction site BstEII and SgrA1 (defined as sequence 2) of 5-HT3 receptors is important for the binding affinity of clozapine.
Analysis of 5-HT activation curves and clozapine inhibition curves using the Cheng-Prusoff equation revealed an extracellular sequence (length 86 aa) close to the transmembrane domain M1 which strongly determines the binding affinity of clozapine.
The use of the Cheng-Prusoff equation to calculate the dissociation constant Kb values for clozapine revealed that an extracellular sequence (length 86 aa) close to the transmembrane domain M1 strongly determines the binding affinity of clozapine.
Estimation of Kb values for clozapine using the Cheng-Prusoff relationship revealed that sequence 2 of the extracellular ligand binding site (length 86 aa) close to the transmembrane domain M1 strongly determines the binding affinity of clozapine.
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However, the binding affinity of PDZ domains is known to be regulated through allosteric interactions49.
This, in turn, increases the binding affinity of the intracellular domains of the receptor for arrestin proteins.
(B) The binding affinity of NADH toward LDHA was analyzed using Cibacron Blue as a mimicking probe of NADH.
Similarly, the binding affinity of pyruvate to LDHA in the presence of PSTMB was examined using 14C radio-labeled pyruvate.
The binding affinity of CDP2 alone is relatively weak, but it enhances the binding of rITF2 to the TH-dyad.
This binding is explained by the broad binding affinity of lectin.
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