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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1989-12-19
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pubmed:abstractText |
Stabilization of fetal bovine serum (FBS) acetylcholinesterase (acetylcholine acetylhydrolase, EC 3.1.1.7) (AChE) and human butyrylcholinesterase (acylcholine acylhydrolase, EC 3.1.1.8) (BuChE) by ligands and inhibitors was studied as a function of physical and chemical perturbation. Denaturation of AChE occurred as a binary exponential function in the temperature range studied (50-56 degrees C); the slower fraction progressively diminished as the temperature was increased. Inclusion of ligands or inhibitors stabilized AChE as a function of temperature, ligand concentration and time. The rank order in which ligands stabilized AChE was: edrophonium greater than decamethonium greater than pralidoxime chloride much greater than procainamide. BuChE denaturation was retarded by ligands in the order: decamethonium greater than procainamide greater than edrophonium greater than pralidoxime. A plot of the quotient of the fast/slow ratio against the log of the 50% inhibitory concentration (I50) for ligands providing substantial protection yielded a linear relation, suggesting that these compounds stabilized AChE by a common mechanism involving the anionic site of the active center. Urea-induced cholinesterase denaturation was also retarded by these ligands.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetylcholinesterase,
http://linkedlifedata.com/resource/pubmed/chemical/Butyrylcholinesterase,
http://linkedlifedata.com/resource/pubmed/chemical/Cholinesterases,
http://linkedlifedata.com/resource/pubmed/chemical/Decamethonium Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Edrophonium,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Pralidoxime Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Procainamide,
http://linkedlifedata.com/resource/pubmed/chemical/pralidoxime
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
999
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
46-51
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2804138-Acetylcholinesterase,
pubmed-meshheading:2804138-Animals,
pubmed-meshheading:2804138-Butyrylcholinesterase,
pubmed-meshheading:2804138-Cattle,
pubmed-meshheading:2804138-Cholinesterases,
pubmed-meshheading:2804138-Decamethonium Compounds,
pubmed-meshheading:2804138-Edrophonium,
pubmed-meshheading:2804138-Enzyme Stability,
pubmed-meshheading:2804138-Humans,
pubmed-meshheading:2804138-Hydrogen-Ion Concentration,
pubmed-meshheading:2804138-Ligands,
pubmed-meshheading:2804138-Pralidoxime Compounds,
pubmed-meshheading:2804138-Procainamide,
pubmed-meshheading:2804138-Temperature
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pubmed:year |
1989
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pubmed:articleTitle |
Ligand stabilization of cholinesterases.
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pubmed:affiliation |
Department of Applied Biochemistry, Walter Reed Army Institute of Research, Washington, DC.
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pubmed:publicationType |
Journal Article,
Comparative Study
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