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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1997-9-4
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pubmed:abstractText |
Solid phase fixed peptides are useful tools for the investigation of enzyme substrate interactions. We could show that interactions of target sequences, like e.g. the acceptor domain of G-proteins for the of mono ADP-ribosylation by pertussis toxin and the toxin itself can be studied by this method. Reaction specificity is identical to modification of free peptides. The method is extremely versatile and has enormous potential if the focus is on the effects of substrate modification or substrate length.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
0065-2598
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
419
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
87-91
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pubmed:dateRevised |
2006-4-17
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pubmed:meshHeading |
pubmed-meshheading:9193640-Adenosine Diphosphate,
pubmed-meshheading:9193640-Adenosine Diphosphate Ribose,
pubmed-meshheading:9193640-Cellulose,
pubmed-meshheading:9193640-GTP-Binding Proteins,
pubmed-meshheading:9193640-Membranes, Artificial,
pubmed-meshheading:9193640-Peptide Fragments,
pubmed-meshheading:9193640-Pertussis Toxin,
pubmed-meshheading:9193640-Structure-Activity Relationship,
pubmed-meshheading:9193640-Substrate Specificity,
pubmed-meshheading:9193640-Virulence Factors, Bordetella
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pubmed:year |
1997
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pubmed:articleTitle |
Membrane anchored synthetic peptides as a tool for structure-function analysis of pertussis toxin and its target proteins.
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pubmed:affiliation |
Institut für Infektiologie, Universität Münster, Germany.
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pubmed:publicationType |
Journal Article
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