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Isolation and Crystallization of an Esteroproteolytic Zymogen from Porcine Pancreas

From the ¹ From the Department of Biochemistry, University of Vermont College of Medicine, Burlington, Vermont

A crystalline preparation of an esteroproteolytic zymogen was obtained from porcine pancreas. The physical and catalytic properties of the zymogen indicate that it is the precursor of an esteroproteolytic enzyme previously isolated and characterized in this laboratory. Activation of the zymogen by trypsin appears to involve only slight proteolysis to produce an enzyme having the same specific activity as the esteroproteolytic enzyme.

The isolation procedure for the esteroproteolytic zymogen included an elution of proteins from a diethylaminoethyl cellulose column by means of a decreasing pH gradient. Under these conditions an anionic precursor of a new proteolytic enzyme with potential tryptic activity was revealed. The chromatographic behavior of the precursor closely parallels that of the esteroproteolytic zymogen. The precursor is both a potential activator and a tenacious contaminant of the esteroproteolytic zymogen. The isolation procedure for the esteroproteolytic zymogen was designed to effect maximum separation and inhibition of the precursor and its active enzyme.

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