Volume 119, Issue 2, Pages (August 2000)

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Volume 119, Issue 2, Pages 461-465 (August 2000) Chronic pancreatitis associated with an activation peptide mutation that facilitates trypsin activation Niels Teich, Johann Ockenga, Albrecht Hoffmeister, Michael Manns, Joachim Mössner, Volker Keim Gastroenterology Volume 119, Issue 2, Pages 461-465 (August 2000) DOI: 10.1053/gast.2000.9312 Copyright © 2000 American Gastroenterological Association Terms and Conditions

Fig. 1 Pedigree of a family with chronic pancreatitis and D22G mutation of the cationic trypsinogen. The patients with documented chronic pancreatitis are represented by closed symbols; individuals with suspected disease are depicted in grey. *D22G variant present. Gastroenterology 2000 119, 461-465DOI: (10.1053/gast.2000.9312) Copyright © 2000 American Gastroenterological Association Terms and Conditions

Fig. 2 HPLC separation of oligopeptide digests. (A) Wild-type peptide (pWT), no trypsin; (B) pWT, 30 minutes of trypsin; (C) pD22G, 30 minutes of trypsin; (D) pK23R, 30 minutes of trypsin. Arrows indicate the position of the octapeptide. Gastroenterology 2000 119, 461-465DOI: (10.1053/gast.2000.9312) Copyright © 2000 American Gastroenterological Association Terms and Conditions

Fig. 3 pH-dependent hydrolysis of synthetic peptides by trypsin. Wild-type (pWT) and mutant (pD22G, pK23R) peptides were incubated with or without trypsin for 30 minutes. After chromatographic separation of the hydrolytic products, the percentage of peptide digestion was measured by integration of the areas under the respective peaks. Values are means ± SE; n = 4; *P < 0.05. Gastroenterology 2000 119, 461-465DOI: (10.1053/gast.2000.9312) Copyright © 2000 American Gastroenterological Association Terms and Conditions

Fig. 4 Mutations and proposed pathogenetic models of hereditary pancreatitis. Gastroenterology 2000 119, 461-465DOI: (10.1053/gast.2000.9312) Copyright © 2000 American Gastroenterological Association Terms and Conditions