dissociation constant


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dis·so·ci·a·tion con·stant (Kd, K),

the equilibrium constant involved in the dissociation of a compound into two or more compounds or ions. The reciprocal of the association constant (2).
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After that, we measured and calculated the apparent dissociation constants ([Kd.sub.app]) of PPAR[beta]/[delta] bound to commercial agonists GW0742 (1.2 [+ or -] 0.3 [micro]M), GW501516 (1.8 [+ or -] 0.1 [micro]M), and L-165,041 (1.09 [+ or -] 0.08 [micro]M) (Figure 5(c)).
Determination of dissociation constants and specific rate constants of enzyme--substrate (or protein--ligand) interactions from rapid reaction kinetic data.
In the latter case, however, the inhibition constants are no longer true dissociation constants but rather complex functions of several individual dissociation constants.
The association dissociation constants are here denoted by k and l, respectively
Due to the lack of information on the equilibrium dissociation constants of Fe-itaconic acid and Al-itaconic acid complexes in the literature, their pK values will be indirectly estimated in the present study.
Table 1: Stern-Volmer constant ([K.sub.SV]), bimolecular quenching rate constant ([K.sub.q]), number of binding sites (n), binding constant ([K.sub.b]), and dissociation constant ([K.sub.d]) of several flavonoid-PDIA3 systems.
Therefore, it is a function of the dissociation constant ([K.sub.d]), the amount of B, and [[A].sub.0].
Acid dissociation constants of the thiohydantoin-pyrrolidine compounds containing methyl ester group as a substituent (1a-g), prepared according to the literature method [25], were determined potentiometrically at 25.0 ([+ or -] 0.1)[degrees]C in a 20% (v/v) ethanol-water mixture.
This change of the binding properties is quantified by a 10-fold decrease of the enzyme-substrate complex dissociation constants, which is sufficient for the generation of cooperativity of the enzyme.
A dissociation constant of 58 nM for a region of the insulin enhancer element was determined by the electrophoretic mobility shift assay.
Removal of the hydroxyl group of Tyr6 has no effect on the dissociation constant for glutathione.
Data for the binding of recombinant rgp 120 to rCD4 gave a dissociation constant of 17 nM, which agrees well with the value of 19 nM previously reported by Wu et al.