Linked Life Data

1139004

Source:http://linkedlifedata.com/resource/pubmed/id/1139004

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1975-9-18
pubmed:abstractText
15 acetoxyethylenammonium compounds are studied as substrates for acetylcholinesterase (ACE) from bovine erythrocytes and for butyrylcholinesterase (BCE) from horse serum. Substitution of methyl groups of the ammonium grouping with other radicals and incorporation of onium nitrogen in the cycle resulted in the decrease of the hydrolysis rate under the action of BCE and ACE, the effect of BCE being more pronounced. The rate of the hydrolysis of N-acetoxyethylene-N-methylpiperidine iodide in the presence of ACE was 65 times as much as in the presence of BCE. This compound is a new specific substrate of ACE. Dipropylmethyl derivative turned not to be a good substrate for both enzymes. Dibutylmethyl and pyridinic derivatives were not attacked by ACE and BCE. Kinetic analysis of the compounds listed is performed, taking account of non-productive sorbtion. Possible role of hydrofobic regions in the orientation of substrates on the active surface of ACE and BCE is discussed.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0320-9725
pubmed:author
pubmed:issnType
Print
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
95-102
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:articleTitle
[Cholinesterase hydrolysis of acetylcholine derivatives with different structures of the ammonium grouping].
pubmed:publicationType
Journal Article, English Abstract