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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1989-10-3
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pubmed:abstractText |
The monoclonal antibody (mAb) AE-2 decreases the rate of hydrolysis of acetylthiocholine (ATC) by fetal bovine serum acetylcholinesterase (acetylcholine acetylhydrolase EC 3.1.1.7) (FBS-AChE) (Doctor, B.P. et al. (1989) Proc. 32nd Oholo Conf., Eilat, Israel, in press), but increases the rate of hydrolysis (Vmax) of the nonpolar substrate, indophenyl acetate (IPA) approx. 15-fold. The affinity (Km) of FBS-AChE for IPA changes minimally in comparison with the increase in the rate of hydrolysis. The complex is dissociated, and the modulation of substrate hydrolysis is reversed by the active-center ligand, 1-methyl-2-hydroxyiminomethylpyridinium chloride (2-PAM).
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
997
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
232-5
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading | |
pubmed:year |
1989
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pubmed:articleTitle |
The monoclonal antibody AE-2 modulates fetal bovine serum acetylcholinesterase substrate hydrolysis.
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pubmed:affiliation |
Department of Applied Biochemistry, Walter Reed Army Institute of Research, Washington, DC 20307-5100.
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pubmed:publicationType |
Journal Article
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