Source:http://linkedlifedata.com/resource/pubmed/id/11412985
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
2001-6-19
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pubmed:abstractText |
Epinephrine (Epi) acts as a neurotransmitter in the brain, but its function therein is not well understood. Phenylethanolamine N-methyltransferase (PNMT) catalyzes the final step in the biosynthesis of Epi and is thus a pharmacological target to investigate the function of Epi in the central nervous system. The kinetic differences between bovine adrenal PNMT and human brain PNMT for a number of substrates and inhibitors are examined and the results reported.
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pubmed:grant | |
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 |
Jun
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pubmed:issn |
0960-894X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1579-82
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11412985-Animals,
pubmed-meshheading:11412985-Cattle,
pubmed-meshheading:11412985-Epinephrine,
pubmed-meshheading:11412985-Humans,
pubmed-meshheading:11412985-Kinetics,
pubmed-meshheading:11412985-Models, Molecular,
pubmed-meshheading:11412985-Phenylethanolamine N-Methyltransferase,
pubmed-meshheading:11412985-Recombinant Proteins,
pubmed-meshheading:11412985-Stereoisomerism,
pubmed-meshheading:11412985-Structure-Activity Relationship,
pubmed-meshheading:11412985-Substrate Specificity
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pubmed:year |
2001
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pubmed:articleTitle |
Phenylethanolamine N-methyltransferase kinetics: bovine versus recombinant human enzyme.
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pubmed:affiliation |
Department of Medicinal Chemistry, University of Kansas, 4060 Malott Hall, 1251 Wescoe Hall Drive, Lawrence, KS 66045-7582, USA. ggrunewald@ukans.edu
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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