Abstract
Recently Luthy et al [1] investigated the mechanism of the interaction between soybean trypsin inhibitor (STI)1 and trypsin by kinetic methods. These authors found that only at very low reactant concentration the reaction is second order with rate constants k on and k off. Significant deviation at higher total enzyme and inhibitor concentrations lead to the postulation of a more complex mechanism with an intermediate complex L which is in fast pre-equilibrium with enzyme E and inhibitor I
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Abbreviations
- PTI:
-
pancreatic trypsin inhibitor (Kunitz)
- STI:
-
soybean trypsin inhibitor (Kunitz)
- NPABC:
-
p-nitrophenyl-N2-acetyl-N1-benzy1carbazate
References
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Engel, J., Quast, U., Heumann, H., Krause, G., Steffen, E. (1974). Kinetic Studies of the Binding of Bovine Basic Pancreatic Trypsin Inhibitor to α-Chymotrypsin. 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_46
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