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Membrane Anchored Synthetic Peptides as a Tool for Structure-Function Analysis of Pertussis Toxin and its Target Proteins

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 419))

Abstract

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 specifity is identical to modification of free peptides. The method is extremly versatile and has enourmous potential if the focus is on the effects of substrate modification or substrate length.

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References

  1. Graf, R., Codina, J., and Birnbaumer, L. 1992. Peptide inhibitors of ADP-ribosylation by Pertussis toxin are substrates with affinities comparable to those of the trimeric GTP-binding proteins. Molecular pharmacology 42: 760–764.

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  2. Frank, R. 1992. Spot synthesis: An easy technique for the positionally addressable, parallel chemical synthesis on membrane support. Tetrahedron 48: 9217–9232.

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  3. von Olleschik-Elbheim, L., el Bayâ, A., and Schmidt, MA. 1996. Positional analysis of the C-terminal acceptor site of Gi proteins for pertussis toxin mediated ADP-ribosylation. Journal of Biological Chemisty. submitted.

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© 1997 Springer Science+Business Media New York

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von Olleschik-Elbheim, L., el Bayâ, A., Alexander Schmidt, M. (1997). Membrane Anchored Synthetic Peptides as a Tool for Structure-Function Analysis of Pertussis Toxin and its Target Proteins. In: Haag, F., Koch-Nolte, F. (eds) ADP-Ribosylation in Animal Tissues. Advances in Experimental Medicine and Biology, vol 419. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-8632-0_10

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  • DOI: https://doi.org/10.1007/978-1-4419-8632-0_10

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-4652-4

  • Online ISBN: 978-1-4419-8632-0

  • eBook Packages: Springer Book Archive

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