Kinetic evidence for a two-step mechanism for the binding of chymotrypsin to alpha 1-proteinase inhibitor. |
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| Authors: | M Bruch and J G Bieth |
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| Institution: | Laboratoire d'Enzymologie, Faculté de Pharmacie, Université Louis Pasteur de Strasbourg, France. |
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| Abstract: | We have used the proflavin displacement method and a stopped-flow apparatus to measure the rate constant for the binding of 2 microM-chymotrypsin to 20-125 microM-alpha 1-proteinase inhibitor. The observed pseudo-first-order constant showed a hyperbolic dependence on alpha 1-proteinase inhibitor concentration, suggesting a reaction mechanism in which a fast pre-equilibrium (K = 0.19 mM) is followed by a first-order formation of the final complex (k = 252 s-1). |
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