Kinetics of alpha-chymotrypsin dimerization.
A method has been devised which permits the observation of the loss of active sites promoted by aggregation of alpha-chymotrypsin. When alpha-chymotrypsin in unbuffered solution at pH 7 is mixed with buffered proflavin by stopped flow instrumentation to give a final pH of 3.89, a decrease in active sites occurs, as measured by a decrease in enzyme-dye complex. The decrease in the rate of active sites shows a linear dependence on the square of the concentration of active sites remaining at equilibrium. The kinetic data of the reaction have been correlated with equilibrium measurements. Rate constants for formation and dissociation of dimer are 9.45 X 10(3) M(-1)S(-1) and 1.9 S(-1),, respectively. Calculation of Kdis for dimer from rate constants gives a value of 2.01 X 10(-4) M, while direct determination of Kdis gives a value of 1.44 X 10(-4) M.[1]References
- Kinetics of alpha-chymotrypsin dimerization. Gilleland, M.J., Bender, M.L. J. Biol. Chem. (1976) [Pubmed]
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