Ligand-receptor interactions kinetics

A lack of agreement between the Kj estimated in equilibrium experiments and that determined in kinetic experiments (k i/ki = Kd) suggests a more complex ligand-receptor interaction. 

CEP receptors exhibit high ligand affinity and saturation kinetics for ligand binding. The protein portion of these complexes appears to participate in ligand-receptor interaction since protease treatment of aortic CEP complexes abolishes uptake [24]. Binding is competitively inhibited by polyanions in a pattern similar to the inhibition observed for the acetyl-LDL receptor [24]. However, the CEP receptor appears to be distinct from the acetyl-LDL receptor since their ligands do not mutually compete for uptake [24]. 

Principle 1 a defined endpoint biological activity, then generalized to the final product rate in the ligand-receptor interaction, as based on the Michaelis-Menten enz34ne-substrate kinetics ... 

Not only do these studies support the presence in blood platelets of receptors with two distinct binding affinities but s concept is also supported by earlier functional evidence that thrombin-induced platelet activation is mediated by two distinct pathways which differ in their sensitivity to proteolysis, their requirement for sodium ions, in the need for receptor occupancy and in the role of G proteins (reviewed in ). Furthermore, kinetic studies demonstrated that both ligand-receptor and proteolytic interactions occur in thrombin-induced platelet activation. Thus, foe preponderance of evidence supports foe view that two different types of receptor are involved in foe interaction of thrombin with platelets. The major question is, however, what is foe nature of these two receptors ... 

Binding partners and their interaction kinetics (e.g., to bind a receptor antigen, an antagonistic mAb will have to compete with the endogenous ligand)... 

Cheskis, B., and Freedman, L. P. Modulation of nuclear receptor interactions by ligands Kinetic... 

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