The dissolution rate is K(dissociation) = 8.93 × 10 ⁻⁵ s⁻¹.
It is given that
The dissolution rate, [tex]$\mathrm{k}($[/tex] association [tex]$)=8.93 \times 10^3 \mathrm{M}^{-1} \mathrm{~s}^{-1}$[/tex]
The value of overall dissolution constant [tex]$\mathrm{K}_{\mathrm{d}}=10 \mathrm{~nm}=10 \times 10^{-9} \mathrm{M}$[/tex]
Now,
The dissociation constant [tex]$(\mathrm{Kd})$[/tex] is given as:
[tex]$K_d=\frac{k(\text { dissociation })}{k(\text { association })}$[/tex]
on substituting the values, we get
[tex]$10 \times 10^{-9}=\frac{k(\text { dissociation })}{8.93 \times 10^3}$[/tex]
[tex]$K($[/tex] dissociation [tex]$)=8.93 \times 10^{-5} \mathrm{~s}^{-1}$[/tex]
The rate or speed at which a ligand separates from a protein, such as a receptor, is known as the dissociation rate in the fields of chemistry, biochemistry, and pharmacology. It plays a significant role in the intrinsic activity (efficacy) and binding affinity of a ligand at a receptor.
The Michaelis-Menten model of enzyme kinetics can be used to determine the dissociation rate for a specific substrate. How fast or slowly the substrate dissociates influences the size of the enzyme's velocity.
The enzyme binds to the substrate in the Michaelis-Menten model, resulting in an enzyme-substrate complex that can either proceed forward by creating a product or backward by dissociating. Using Koff, the dissociation rate constant is described.
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