Abstract
The basic trypsin-kallikrein inhibitor (Kunitz) of bovine organs was the first inhibitor to be purified [1], elucidated in its covalent structure [2–9] and in its atomic structure [10, 11]. The kinetics of complex association upon inhibition of trypsin[12] and of chymotrypsin [12–14] have been investigated. Because of its broad specificity this inhibitor has found wide use in therapeutical applications [15].
Supported by the Deutsche Forschungsgemeinschaft, Bonn-Bad Godesberg, and the Fonds der Chemischen Industrie, Frankfurt.
Part of the Ph. D.-thesis, H. Jering, Technische Universität München 1973.
The animal experiments were performed in the Institute für Klinische Chemie und Klinische Biochemie, Universität München.
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References
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Tschesche, H., Jering, H., Schorp, G., Dietl, T. (1974). Reactive Site Cleavage, Thermodynamic Control Resynthesis, and Properties of Chemically Derivatized Trypsin-Kallikrein-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_42
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