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The Characterization of Rat Pancreatic Zymogens and Their Active Forms by Gel Diffusion Techniques

Jane Pascale 1, Stratis Avrameas 1, and José Uriel 1

From the 1 From the Laboratoire de Chimie des Protéines, Institut de Recherches Scientifiques sur le Cancer, Villejuif (Seine), France

The antigenic constituents in activated and nonactivated rat pancreatic extracts have been demonstrated by immunoelectrophoresis. Specific reactions with appropriate substrates have been used to identify and to localize the zymogens and their active forms on the immunoelectrophoretic diagrams.

In the activated extracts, elastase, alpha-amylase, ribonuclease, carboxypeptidase B, chymotrypsin, and lipase have been identified as single antigens. Two immunologically distinct enzymes with carboxypeptidase A activity, as well as two others with trypsin activity, have been demonstrated.

The following zymogens have been identified: one proelastase, one chymotrypsinogen, one procarboxypeptidase B and two immunologically distinct trypsinogens. The procarboxypeptidase A appears as two electrophoretic fractions with common antigenic properties.

From the two trypsinogens derive two immunologically distinct trypsins. The procarboxypeptidase A gives rise after activation to two immunologically distinct carboxypeptidases A.

Submitted on December 16, 1965


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Copyright © 1966 by the American Society for Biochemistry and Molecular Biology.
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