Analysis of human exocrine pancreatic proteins by means of pore gradient polyacrylamide gel electrophoresis.

Pancreatic juice collected by endoscopic retrograde cannulation of the pancreatic duct after administration of secretin and pancreozymin was analyzed by pore gradient polyacrylamide gel electrophoresis. Two electrophoretic systems, an alkaline (pH 8.9) and an acidic (pH 5.0), were elaborated to obtain optimal separation of exocrine proteins. 13 bands under alkaline conditions and 17 bands by running in the acidic system were separated and distinguished by Coomassie-Brilliant Blue G 250 staining. Fourteen proteins were identified using enzymatic and immunological methods: one form of each of lipase, chymotrypsinogen, prophospholipase A2, procarboxypeptidase A and trypsin inhibitor, two forms of each of procarboxypeptidase B and proelastase, three forms of each of trypsinogen and amylase. An additional band was identified as albumin.