Trypsinogen, PMSF treated from bovine pancreas

Trypsinogen, PMSF treated from bovine pancreas has been used as a non-phosphorylated control to analyze the phospho-protein α-casein from bovine milk by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). It has also been used as a molecular weight marker standard in SDS-PAGE.

Trypsinogen is a pancreatic proteinase and exists as isoenzymes 1 and 2. It is an inactive precursor of trypsin and gets activated by the enteropeptidase found on the brush border membrane of enterocytes in the duodenum. It is also known to proteolytically activate itself. Trypsinogen activation is associated with acute pancreatitis as it causes pancreatic enzyme cascade which activates the remaining zymogens leading to autodigestion of the neighboring tissue. Hereditary pancreatitis was shown to be caused by a Arg-His substitution at residue 117 of trypsinogen causing auto-activation of trypsinogen to trypsin.