LOCALIZATION BY IMMUNOFLUORESCENCE OF AMYLASE, TRYPSINOGEN AND CHYMOTRYPSINOGEN IN THE ACINAR CELLS OF THE PIG PANCREAS

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Abstract
The localization of α-amylase in the pig pancreas, and of chymotrypsinogen and trypsinogen in the beef pancreas, has been investigated by immunofluorescence, using antisera prepared in rabbits against commercial crystalline enzyme preparations. Porcine α-amylase was abundant in almost every acinar cell, being distributed as fine granular material in the basal part of the cell, and also in some of the zymogen granules in the juxta-nuclear region. It was visible also in the Golgi zone. Bovine chymotrypsinogen and trypsinogen were present in the presumably less mature zymogen granules in the cytoplasm around the nucleus, but the granules near the lumen failed to react with the antisera, perhaps because they were hidden by superficial material. The specificity of the anti-amylase serum was high, that of the anti-chymotrypsinogen and anti-trypsinogen lower because of cross reactions with each other. In both porcine and bovine pancreas, the acinar cells were virtually all similar, indicating functional similarity to the extent of these observations.