Kinetic properties of carboxypeptidase B in solutions and crystals.

The correlation of the structure of crystalline enzymes with their activities in solution assumes that the catalytic properties are identical in the two physical states. The present data demonstrate that in bovine carboxypeptidase B they differ significantly. Normal Michaelis-Menten kinetics characterize the hydrolysis of several esters and peptide substrates in both physical states.

A general computer approach for calculating rate constants from near-equilibrium kinetic studies.

A general computer approach for estimating rate constants from relaxation times is described. The programme CORNEK is essentially a least-squares refinement programme applied to non-linear systems. It uses directly the differential forms of the first derivatives of mass-balance and rate equations, thus avoiding the time-consuming derivations of near-equilibrium rate equations.