A number of peptides derivatives were found to increase the peptides activity of caboxypeptidase A towards benzyloxycarbonyl‐depeptides. The accelerators are either completely resistant to cleavage by carboxypeptidase A or degraded at a very slow rate. To evaluate the mode of action of the activators (A), the kinetics of hydrolysis of the substrate (S) by the enzyme (E) was followed by measuring the effect of a constant concentration of A on varying concentrations of S and vice versa. These studies indicate that an EA complex is formed, and that EA reacts with S to form an active ternary complex, EAS. Acceleration is observed because EA has a higher affnity for S than the free enzyme. Ultracentrifuge studies show that The activators do not induce aggregation of carboxypeptidase A.
No takes yet. Share an insight, caveat, or question.
Schechter et al. (1971) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: