Biomaterial Database

[Estimation of anticholinesterase activity in reversible inhibitors of cholinesterase hydrolysis]. 1994

A P Brestkin, and L P Kuznetsova, and E V Rozengart

The kinetic analysis of cholinesterase interaction with reversible inhibitors was carried out. It has shown that the existing methods for definition of the type of reversible inhibition of enzyme reactions are not reliable. For example, mixed inhibition with the correlation between the competitive inhibition constant (Kl) and noncompetitive inhibition constant (K'i) less than 0.04, is identified as competitive inhibition. Apparently the ideal competitive inhibition with Ki/Ki = 0 does not exist in reality, because it is unlikely for a reversible inhibitor to decrease the process of the substrate sorption on a catalytical centre of cholinesterase not affecting the deacetylation rate. For objective evaluation of efficiency of reversible inhibitors it is suggested to determine the generalized inhibitory constant Ki at the cholinesterase hydrolysis in acetylcholine or acetylthiocholine. The data about anticholinesterase activity of carbonic and sulfoesters of lupinin are adduced.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D002384	Catalysis	The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.	Catalyses
D002800	Cholinesterase Inhibitors	Drugs that inhibit cholinesterases. The neurotransmitter ACETYLCHOLINE is rapidly hydrolyzed, and thereby inactivated, by cholinesterases. When cholinesterases are inhibited, the action of endogenously released acetylcholine at cholinergic synapses is potentiated. Cholinesterase inhibitors are widely used clinically for their potentiation of cholinergic inputs to the gastrointestinal tract and urinary bladder, the eye, and skeletal muscles; they are also used for their effects on the heart and the central nervous system.	Acetylcholinesterase Inhibitor,Acetylcholinesterase Inhibitors,Anti-Cholinesterase,Anticholinesterase,Anticholinesterase Agent,Anticholinesterase Agents,Anticholinesterase Drug,Cholinesterase Inhibitor,Anti-Cholinesterases,Anticholinesterase Drugs,Anticholinesterases,Cholinesterase Inhibitors, Irreversible,Cholinesterase Inhibitors, Reversible,Agent, Anticholinesterase,Agents, Anticholinesterase,Anti Cholinesterase,Anti Cholinesterases,Drug, Anticholinesterase,Drugs, Anticholinesterase,Inhibitor, Acetylcholinesterase,Inhibitor, Cholinesterase,Inhibitors, Acetylcholinesterase,Inhibitors, Cholinesterase,Inhibitors, Irreversible Cholinesterase,Inhibitors, Reversible Cholinesterase,Irreversible Cholinesterase Inhibitors,Reversible Cholinesterase Inhibitors
D002802	Cholinesterases		Acylcholineacylhydrolase,Cholase,Cholinesterase
D006868	Hydrolysis	The process of cleaving a chemical compound by the addition of a molecule of water.
D001665	Binding Sites	The parts of a macromolecule that directly participate in its specific combination with another molecule.	Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D001667	Binding, Competitive	The interaction of two or more substrates or ligands with the same binding site. The displacement of one by the other is used in quantitative and selective affinity measurements.	Competitive Binding
D013329	Structure-Activity Relationship	The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.	Relationship, Structure-Activity,Relationships, Structure-Activity,Structure Activity Relationship,Structure-Activity Relationships
D015394	Molecular Structure	The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.	Structure, Molecular,Molecular Structures,Structures, Molecular