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The Use of Fluorescence Techniques in the Study of the Interaction of the Basic Trypsin Inhibitor of Bovine Pancreas, Selectively Labelled at Lysine 15, with Chymotrypsin and Trypsin

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Proteinase Inhibitors

Part of the book series: Bayer-Symposium ((BAYER-SYMP,volume 5))

Abstract

Fluorescence techniques are particularly suitable for the study of the interaction between two different proteins, one of which does not possess tryptophan. A fluorescent label attached to such a component may be used as an independent probe of the polarity, symmetry and rigidity of its environment, or as an energy acceptor from tryptophans of the protein molecule with which it interacts. Tryptophan is excited at around 280 nm and has a fluorescence emission spectrum with a maximum around 350 nm. A group with an absorption spectrum which overlaps with this fluorescence spectrum (and which fluoresces at a higher wavelength range) may act as an energy acceptor.

Presented by Meir Rigbi.

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Abbreviations

BPTI:

basic pancreatic trypsin inhibitor

AMI:

anthraniloyl (Lys 15) maleylated BPTI

DMI:

didansyl (Lys 15. Tyr) maleylated BPTI

References

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Author information

Authors and Affiliations

  1. Department of Biological Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel

    Y. Elkana

Authors
  1. Y. Elkana
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Editor information

Editors and Affiliations

  1. Institut für Klinische Chemie und Klinische Biochemie, Universität München, 8000, Munich 2, Fed. Rep. Germany

    Hanz Fritz

  2. Organisch-Chemisches Laboratorium, Technischen Universität München, 8000, Munich 2, Fed. Rep. Germany

    Harald Tschesche

  3. Department of Biology, Brookhaven National Laboratory, Upton, NY, 11973, USA

    Lewis J. Greene

  4. Biochemisches Laboratorium, Bayer AG, 5600, Wuppertal 1, Fed. Rep. Germany

    Ernst Truscheit (Editor-in-Chief) (Editor-in-Chief)

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© 1974 Springer-Verlag

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Elkana, Y. (1974). The Use of Fluorescence Techniques in the Study of the Interaction of the Basic Trypsin Inhibitor of Bovine Pancreas, Selectively Labelled at Lysine 15, with Chymotrypsin and Trypsin. In: Fritz, H., Tschesche, H., Greene, L.J., Truscheit, E. (eds) Proteinase Inhibitors. Bayer-Symposium, vol 5. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-87966-1_49

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  • DOI: https://doi.org/10.1007/978-3-642-87966-1_49

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-87968-5

  • Online ISBN: 978-3-642-87966-1

  • eBook Packages: Springer Book Archive

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