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Kinetics and Thermodynamics of the Interaction of Proteinases with Protein Inhibitors

  • Conference paper
Proteinase Inhibitors

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

Abstract

This presentation bears a striking resemblance to the one given at the First International Research Conference on Proteinase Inhibitors [1]. It appears that the development of an adequate mechanism for the enzyme-inhibitor interaction and of convenient techniques for obtaining values of the kinetic and thermodynamic parameters appearing in this mechanism will be a slow, ongoing process. However, as the rough details of the mechanism are understood it becomes possible to see more clearly that many protein proteinase inhibitors interact with proteinases by a very closely similar mechanism. This is most dramatically illustrated by the X-ray crystallographic studies which show that the stable complex of trypsin with two very different inhibitors involves virtually identical interactions. This similarity in main aspects of the interactions offers an opportunity for interpreting some of the observed differences between inhibitors in detailed molecular terms. A small beginning is made in this paper.

Supported by Grants GM 10831 and GM 11812 from the National Institutes of Health, U. S. Public Health Service.

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Author information

Author notes

  1. M. A. Hamid

    Present address: Department of Biochemistry, University of Libya, Faculty of Medicine, Benghazi, Libya

  2. R. W. Sealock

    Present address: Neurobiologie Moleculaire, Institut Pasteur, Paris, France

  3. D. Wang

    Present address: Florida A&M University, Tallahassee, Florida, 32307, USA

Authors and Affiliations

  1. Department of Chemistry, Purdue University, West Lafayette, IN, 47907, USA

    W. R. Finkenstadt, M. A. Hamid, J. A. Mattis (National Science Foundation Predoctoral Trainee), J. Schrode (National Institutes of Health Predoctoral Trainee), R. W. Sealock, D. Wang & M. Laskowski Jr.

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  1. W. R. Finkenstadt
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  2. M. A. Hamid
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  3. J. A. Mattis
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  4. J. Schrode
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  5. R. W. Sealock
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  6. D. Wang
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  7. M. Laskowski Jr.
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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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Finkenstadt, W.R. et al. (1974). Kinetics and Thermodynamics of the Interaction of Proteinases with Protein Inhibitors. 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_45

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  • DOI: https://doi.org/10.1007/978-3-642-87966-1_45

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-87968-5

  • Online ISBN: 978-3-642-87966-1

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