A rapid method for the detection of trypsinogen and chymotrypsinogen after electrophoretic separation of pancreas extract on polyacrylamide gel

Abstract

Several methods have been described for the visualization of proteolytic activity on electropherograms obtained with starch (1,2), agar and agarose (3–6), paper (7), and cellulose acetate (8–11) as supporting media. In most of these reports casein was used as a (nonspecific) substrate. In only one case (11), the authors used substrates specific for trypsin and for chymotrypsin.

The proteins in a pancreas extract could be satisfactorily separated by electrophoresis on polyacrylamide gel and we looked for the possibility of localizing proteolytic activities in this gel.

Recently (12,13) methods for the direct localization of proteolytic activity in polyarcylamide gels were published, but no attempt was made in these articles to distinguish between trypsin and chymotrypsin. In this paper we will describe a method for the detection of Tg1 and ChTg after their activation in the polyacrylamide gel. The method allows a rapid and reliable localization of the two proenzymes.