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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1998-8-31
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pubmed:abstractText |
Nonspecific protein binding is a commonly encountered problem with synthetic molecules designed as enzyme inhibitors. When the substrate for the enzymatic reaction is itself a protein, such nonspecific protein binding can also occur. Here, we demonstrate that this phenomenon can have a dramatic effect on the steady-state kinetic evaluation of such inhibitors.
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pubmed:commentsCorrections | |
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 |
0006-2952
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
55
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1785-90
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pubmed:dateRevised |
2000-12-18
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pubmed:meshHeading |
pubmed-meshheading:9714296-Catalysis,
pubmed-meshheading:9714296-Dose-Response Relationship, Drug,
pubmed-meshheading:9714296-Enzyme Inhibitors,
pubmed-meshheading:9714296-Enzymes,
pubmed-meshheading:9714296-Kinetics,
pubmed-meshheading:9714296-Models, Biological,
pubmed-meshheading:9714296-Protein Binding
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pubmed:year |
1998
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pubmed:articleTitle |
Kinetic effects due to nonspecific substrate-inhibitor interactions in enzymatic reactions.
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pubmed:affiliation |
Department of Chemical Enzymology, The DuPont Merck Research Laboratories, Wilmington, DE 19880-0400, USA. Copelara@lldmpc.dnet.dupont.com
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pubmed:publicationType |
Journal Article
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