Linked Life Data

3968080

Source:http://linkedlifedata.com/resource/pubmed/id/3968080

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1985-3-18
pubmed:abstractText
Tetranitromethane inhibits acetylcholinesterase with respect to the hydrolysis of both acetylthiocholine and indophenyl acetate. The loss of activity with indophenyl acetate, a poor substrate, is preceded by an increase in enzyme activity. Only 12 of the 21 tyrosine residues/monomer of enzyme are susceptible to nitration. Loss of activity with respect to indophenyl acetate occurs well after no further nitration of tyrosines occurs and must be due to the modification of other residues. Incubation of the enzyme with arsenite before nitration results in the nitration of only 10 tyrosines. This experiment reveals that the structural basis for the binding of arsenite is the formation of a diester with two tyrosine residues.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
260
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1475-8
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Acetylcholinesterase: inhibition by tetranitromethane and arsenite. Binding of arsenite by tyrosine residues.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.