EC50 Reaction dependent. The molar concentration of
an agonist, which produces 50% of the maximum possible
response for that agonist under the stated conditions.
Unit M.
IC50 Reaction dependent. The molar concentration of
an agonist, which produces 50% of the maximum possible
inhibitory response for that agonist under the stated
conditions. Unit M.
Ki Reaction independent. Equilibrium constant for
inhibitor binding. Unit M
Km the concentration of substrate at which the
reaction rate is equal to half the maximal rate (i.e.
Km={s} when V0=˝Vmax). This definition is not true for
allosteric enzymes. Unit M
Synonym: Michaelis-Menten constant
Kcat the number of substrate molecules converted to
product in a given unit of time on a single enzyme
molecule when the enzyme is saturated with substrate.
Unit. Per second
Synonym: Turnover number
Kd - The equilibrium dissociation constant for a
receptor/ligand, or protein A dissociating from protein
B. Unit M.
Embryonic kinetics CV for your approval/comment.
Kinetics
- Binding kinetics -- Kd -- EC50
EC50 Reaction dependent. The molar concentration of an agonist, which produces 50% of the maximum possible response for that agonist under the stated conditions. Unit M.
IC50 Reaction dependent. The molar concentration of an agonist, which produces 50% of the maximum possible inhibitory response for that agonist under the stated conditions. Unit M.
Ki Reaction independent. Equilibrium constant for inhibitor binding. Unit M
Km the concentration of substrate at which the reaction rate is equal to half the maximal rate (i.e. Km={s} when V0=˝Vmax). This definition is not true for allosteric enzymes. Unit M Synonym: Michaelis-Menten constant
Kcat the number of substrate molecules converted to product in a given unit of time on a single enzyme molecule when the enzyme is saturated with substrate. Unit. Per second Synonym: Turnover number
Kd - The equilibrium dissociation constant for a receptor/ligand, or protein A dissociating from protein B. Unit M.
Reported by: orchard