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In chemistry, biochemistry, and pharmacology, a dissociation constant (K D) is a specific type of equilibrium constant that measures the propensity of a larger object to separate (dissociate) reversibly into smaller components, as when a complex falls apart into its component molecules, or when a salt splits up into its component ions.
Unless the complex is very long lived under gel conditions, or dissociation during electrophoresis is taken into account, the number derived is an apparent Kd. If the protein concentration is not known but the complex stoichiometry is, the protein concentration can be determined by increasing the concentration of DNA probe until further ...
The Hill equation is used extensively in pharmacology to quantify the functional parameters of a drug [citation needed] and are also used in other areas of biochemistry. The Hill equation can be used to describe dose-response relationships, for example ion channel open-probability (P-open) vs. ligand concentration.
56720 Ensembl ENSG00000262635 ENSG00000151790 ENSMUSG00000028011 UniProt P48775 P48776 RefSeq (mRNA) NM_005651 NM_019911 RefSeq (protein) NP_005642 NP_064295 Location (UCSC) Chr 4: 155.85 – 155.92 Mb Chr 3: 81.86 – 81.88 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse In enzymology, tryptophan 2,3-dioxygenase (EC 1.13.11.11) is a heme enzyme that catalyzes the oxidation of L ...
The dissociation rate in chemistry, biochemistry, and pharmacology is the rate or speed at which a ligand dissociates from a protein, for instance, a receptor. [1] It is an important factor in the binding affinity and intrinsic activity (efficacy) of a ligand at a receptor. [1]
The binding constant, or affinity constant/association constant, is a special case of the equilibrium constant K, [1] and is the inverse of the dissociation constant. [2] It is associated with the binding and unbinding reaction of receptor (R) and ligand (L) molecules, which is formalized as:
A ligand binding assay (LBA) is an assay, or an analytic procedure, which relies on the binding of ligand molecules to receptors, antibodies or other macromolecules. [1] A detection method is used to determine the presence and amount of the ligand-receptor complexes formed, and this is usually determined electrochemically or through a fluorescence detection method. [2]
[3] [4] It consists of two cells which are enclosed in an adiabatic jacket. The compounds to be studied are placed in the sample cell, while the other cell, the reference cell, is used as a control and contains the buffer in which the sample is dissolved.