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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
8
|
| pubmed:dateCreated |
1975-11-6
|
| pubmed:abstractText |
The hydrolysis of acetylcholine and acetylcholine mustard by acetylcholinesterase was compared over a substrate concentration range of 1-10 mM. Reactions were allowed to proceed for 2 min at 25 degrees. Results of these experiments reveal that the substrates have similar affinities for the enzyme, whereas the maximum velocity for the hydrolysis of acetylcholine mustard was significantly lower than for acetylcholine. These findings suggest that acetylcholine mustard has the ability to inactive acetycholinesterase.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0022-3549
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
64
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1419-21
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
1975
|
| pubmed:articleTitle |
Interactions of acetylcholine mustard with acetylcholinesterase.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|