Abstract:
:Exocrine proteins contained in human pancreatic juice were analyzed by reversed-phase high performance liquid chromatography (RP-HPLC). Pancreatic juice was saved by endoscopic retrograde cannulation of the main pancreatic duct in 17 persons: 12 without pancreatic disease, 3 patients suffering from recurrent acute pancreatitis probably due to pancreas divisum, 1 patient with a carcinoma of the pancreas, and 1 patient with chronic calcified pancreatitis. The juice proteins were separated on a silica column (Nucleosil 300-7 RP) by use of a multistep acetonitrile/water gradient (+0.1% trifluoroacetic acid). Up to 18 individual peaks could be separated by one analytical run (60 min). Molecular weight analysis by sodium dodecyl sulfate-gel electrophoresis indicated the presence of enzymes such as amylase, prophospholipase A2, procarboxypeptidases, trypsinogens, and chymotrypsinogens in certain peaks. Small residual enzymatic activities correlating with certain peaks were detected for amylase and chymotrypsin, and high residual activities were found for phospholipase A (recovery of enzymatic activity compared with the original sample amounted to 65%). Significant amounts of cathodic trypsin-like immunoreactivity were found in two certain peaks. By always loading 350 micrograms of protein/injection on the column the profiles of various samples showed similar patterns. Repeated injections of aliquots revealed highly reproducible profiles. RP-HPLC offers precise, reproducible, and rapid separation of the major proteins of human pancreatic juice.
journal_name
Pancreasjournal_title
Pancreasauthors
Göke B,Keim V,Dagorn JC,Arnold R,Adler Gdoi
10.1097/00006676-199005000-00004subject
Has Abstractpub_date
1990-05-01 00:00:00pages
261-6issue
3eissn
0885-3177issn
1536-4828journal_volume
5pub_type
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