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Replacements, Insertions, and Modifications of Amino Acid Residues in the Reactive Site of Soybean Trypsin Inhibitor (Kunitz)

  • Conference paper
Proteinase Inhibitors

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

Abstract

In the further attempt to understand the molecular details of the inhibition of proteolytic enzymes by protein inhibitors, our laboratory has undertaken an extensive study of the effects of alterations of specific reactive site amino acid residues on the enzyme-inhibitor interaction. Removals, replacements and insertions of amino acid residues in the reactive site of the soybean trypsin inhibitor (STI) of Kunitz have been carried out as well as chemical modifications of functional groups.

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

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Author information

Author notes

  1. D. Kowalski (Minnesota Minning and Manufacturing Predoctoral Fellow)

    Present address: Laboratory of Enzymology, Roswell Park Memorial Institute, Buffalo, New York, 14203, USA

  2. T. R. Leary (American Cancer Society Postdoctoral Fellow)

    Present address: Department of Biochemistry, University of Washington, Seattle, Washington, 98105, USA

  3. R. W. Sealock (National Science Foundation Predoctoral Fellow)

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

  4. D. Wang

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

Authors and Affiliations

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

    D. Kowalski (Minnesota Minning and Manufacturing Predoctoral Fellow), T. R. Leary (American Cancer Society Postdoctoral Fellow), R. E. McKee, R. W. Sealock (National Science Foundation Predoctoral Fellow), D. Wang & M. Laskowski Jr.

Authors
  1. D. Kowalski
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  2. T. R. Leary
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  3. R. E. McKee
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  4. R. W. Sealock
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  5. D. Wang
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  6. 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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Kowalski, D., Leary, T.R., McKee, R.E., Sealock, R.W., Wang, D., Laskowski, M. (1974). Replacements, Insertions, and Modifications of Amino Acid Residues in the Reactive Site of Soybean Trypsin Inhibitor (Kunitz). 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_38

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  • DOI: https://doi.org/10.1007/978-3-642-87966-1_38

  • 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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