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).
Research Article|May 01 1989
Kinetic evidence for a two-step mechanism for the binding of chymotrysin to α1-proteinase inhibitor
Biochem J (1989) 259 (3): 929-930.
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M Bruch, J G Bieth; Kinetic evidence for a two-step mechanism for the binding of chymotrysin to α1-proteinase inhibitor. Biochem J 1 May 1989; 259 (3): 929–930. doi: https://doi.org/10.1042/bj2590929
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