JBC, Vol. 251, Issue 2, 498-502, Jan, 1976
Kinetics of alpha-chymotrypsin dimerization
M. J. Gilleland and M. L. Bender
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.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
