Abstract

The catalytic properties of synthetic polypeptides containing L-amino acids with the sequences H-(His-Glu)n-OH, H-(Ser-Glu)n-OH, H-(His-Tyr)n-OH, and H-(Trp-Glu)n-OH in the hydrolysis of p-NPA (para-nitrophenyl acetate) are considered. The dependences of the rates of the polypeptide-catalyzed hydrolysis of p-NPA on the pH of the medium, the temperature, and the concentration of p-NPA are discussed. Vmax, Km, and K″ — the effective rate constants of the hydrolysis of p-NPA — and K2 — the constant for the splitting out of p-nitrophenol from the substrate — have been found and calculated.

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