In Russia, Ivan Pavlov discovered enteropeptidase, an intestinal protease.
After entering the gut, latent pancreatic proteases were triggered by another enzyme in the upper region of the intestine.
Porcine enteropeptidase from duodenal fluids was partly purified and proven to activate pancreatic extract trypsinogen.
The bovine enteropeptidase light chain's partial amino-terminal sequence was determined via Edman degradation, indicating its similarities to other trypsin-like serine proteases.
Enteropeptidase is fixed to the cell surface via its amino-terminal transmembrane domain.
It is unknown if shedding is a physiological process that controls enteropeptidase activity in the gut.
The process by which the enteropeptidase zymogen is activated is unknown.
Other proteases have been demonstrated to regulate enteropeptidase activity lately.