Electrophoretic separation of proteolytic enzymes in pancreatic juice collected with the pouch or catheter method

Abstract

This qualitative enzyme assay indicated that a considerable amount of chymotrypsin C, anodal trypsin, chymotrypsins A and B, elastase II, and cathodal trypsin were present in samples of nonactivated pancreatic juice from PM pigs. In contrast, the only active enzymes identified in pancreatic juice from CM pigs were very small amounts of chymotrypsin A and elastase II. The amounts of chymotrypsin C and cathodal trypsin were lower in activated than in nonactivated pancreatic juice from PM pigs. However, there were increases in the amounts of the other enzymes when pancreatic juice from PM pigs was activated. As expected, the activation of pancreatic juice from CM pigs resulted in the measurement of very high amounts of all the proteolytic enzymes. The amounts of anodal trypsin, chymotrypsins A and B, and elastase II were higher in activated pancreatic juice from CM pigs than from PM pigs.

Collection of pancreatic juice in experimental animals: mini-review of materials and methods

“…Therefore for illustrative purposes, we recommend the comparison studies: pouch vs Thomas method (Lee et al, 1986) and pouch vs Routley's method (Gabert et al, 1996(Gabert et al, , 1997 undertaken in the same laboratory. Lee et al (1986) (Kiela et al, 1996).…”

“…Lee et al (1986) (Kiela et al, 1996). Electrophoretic separation of proteolytic enzymes showed that in the pancreatic juice collected using pouch method the proteolytic enzymes are near fully active or fully active (Gabert et al, 1997 (Guilloteau et al, 1985, Le Dr6an et al, 1997 …”