Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1982-12-18
pubmed:abstractText
Reversible inhibition of butyrylcholinesterase (acylcholine acylhydrolase, EC 3.1.1.8) with several aroma hydrocarbons was investigated and the results obtained were analyzed in terms of the hydrophobic interaction, making use of the solvent-water partition coefficients for the parameterization of the hydrophobic character of the ligand molecule. To obtain purely hydrophobic effects, the compounds incapable of specific solvation (hydrogen-bond formation) in water as well as in the hydrophobic phase were specially selected for the reaction series. Determination of the hydrophobic properties of the enzyme binding site allows further investigation into the other specificity-determining factors of the non-covalent complex formation step of butyrylcholinesterase-catalyzed reactions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
706
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
174-8
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Reversible inhibition of butyrylcholinesterase with aromatic hydrocarbons.
pubmed:publicationType
Journal Article