Source:http://linkedlifedata.com/resource/pubmed/id/11514231
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
2001-8-21
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pubmed:databankReference | |
pubmed:abstractText |
The stabilization of enzymes in the presence of substrates has been recognized for a long time. Quantitative information regarding this phenomenon is, however, rather scarce since the enzyme destroys the potential stabilizing agent during the course of the experiments. In this work, enzyme unfolding was followed by monitoring the progressive decrease of the rate of substrate utilization by the Staphylococcus aureus PC1 beta-lactamase, at temperatures above the melting point of the enzyme.
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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 |
1074-5521
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
831-42
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11514231-Acylation,
pubmed-meshheading:11514231-Anti-Bacterial Agents,
pubmed-meshheading:11514231-Enzyme Stability,
pubmed-meshheading:11514231-Kinetics,
pubmed-meshheading:11514231-Models, Molecular,
pubmed-meshheading:11514231-Protein Binding,
pubmed-meshheading:11514231-Protein Denaturation,
pubmed-meshheading:11514231-Protein Folding,
pubmed-meshheading:11514231-Staphylococcus aureus,
pubmed-meshheading:11514231-Temperature,
pubmed-meshheading:11514231-Time Factors,
pubmed-meshheading:11514231-beta-Lactamases,
pubmed-meshheading:11514231-beta-Lactams
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pubmed:year |
2001
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pubmed:articleTitle |
Quantitative analysis of the stabilization by substrate of Staphylococcus aureus PC1 beta-lactamase.
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pubmed:affiliation |
Laboratoire d' Enzymologie, Centre d' Ingénierie des Protéines, Institut de Chimie, Université de Liège, Belgium.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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