Pure Human Pancreatic Juice Research Articles

Studies on human pure pancreatic juice collected by endoscopic retrograde catheterization of the papilla.

Pure pancreatic juice was collected from 8 subjects by endoscopic retrograde cannulation of the papilla. Samples were collected at 1 minute intervals for 20 minutes after rapid intravenous injection of secretin (Eisai, 1u/kg) and for 10 to 15 minutes after rapid intravenous injection of CCK-PZ (1 U/kg). Three hydrolases (amylase, chymotrypsinogen and lipase) showed nonparallel secretory pattern. Lipase was proportionally more stimulated than chymotrypsinogen and chymotrypsinogen was more stimulated than amylase by CCK-PZ stimulation. However, in one subject the secretion of three hydrolases was parallel and in another subject lipase and chymotrypsinogen showed parallelism. Samples collected at "wash out" period showed quite high enzyme and protein concentration with specific activity and enzyme ratio not different from those of samples collected at peak period of CCK-PZ stimulation. Normal ranges were estimated in peak flow rate per minute, peak enzyme concentration, specific activity of enzymes, maximal enzyme output per minute and maximal bicarbonate concentration.

Secretin/cholecystokinin-stimulated secretion of trypsinogen and trypsin inhibitor in pure human pancreatic juice collected by endoscopic retrograde catheterization.

Pure pancreatic juice was collected by endoscopic retrograde catheterization of the papilla of Vater from 10 fasting patients without known pancreatic disease. Secretin was given intravenously as a bolus dose at the beginning of the examination and cholecystokinin was given in the same way 15 min later. The juice was siphoned for 25 min and collected in 1-min fractions. Pancreatic secretory trypsin inhibitor, PSTI, and trypsinogen were measured by an immunochemical method. Secretin produced an increase in hydrogencarbonate and a decrease in chloride secretion. Cholecystokinin caused a prompt increase in the concentration of both PSTI and trypsinogen. The ratio between these was constant, suggesting a strictly parallel secretion. The effect of cholecystokinin on secretion of total protein when given as bolus dose was of short duration, with a half-life of action of about 3.5 min.

Cyclic GMP in Pure Human Pancreatic Juice

Cyclic GMP in Pure Human Pancreatic Juice

Bicarbonate and Cyclic Amp Content of Pure Human Pancreatic Juice in Response to Graded Doses of Synthetic Secretin

In seven healthy volunteers pure pancreatic juice was obtained by endoscopic cannulation of the papilla of Vater. Synthetic secretin was intravenously infused in doses doubled every 20 min. The volume of pancreatic juice was proportional to the log of the secretin dose. A significant rise (P less than 0.05) in pancreatic juice flow was elicited at a dose as low as 8.05 ng per kg per hr. Maximum flow rate approximating 250 mul per 5 min per kg of body weight was attained during infusion of 129 ng per kg per hr. At the same dose maximal bicarbonate outputs averaging 383 muEq per hr per kg of body weight were obtained, whereas bicarbonate ion concentration approached peak values (135 +/- 9 muEq per ml) at 32.2 ng per kg per hr. Bicarbonate concentrations showed a tendency to fall at supramaximal doses. The effect of increasing secretin doses on bicarbonate and cyclic AMP concentrations was remarkably similar (rs = 0.635, P less than 0.001) suggesting the participation of cyclic AMP in human pancreatic bicarbonate secretion.

Molecular regulation of digestion: short term and bond specific.

ARTICLESMolecular regulation of digestion: short term and bond specificSS RothmanSS RothmanPublished Online:01 Jan 1974https://doi.org/10.1152/ajplegacy.1974.226.1.77This article has been correctedMoreSectionsPDF (2 MB)Download PDF ToolsExport citationAdd to favoritesGet permissionsTrack citations ShareShare onFacebookTwitterLinkedInWeChat Previous Back to Top Next Download PDF FiguresReferencesRelatedInformation Related ArticlesMolecular regulation of digestion: short term and bond specific 01 Jun 1974American Journal of Physiology-Legacy ContentCited ByPhenylalanine regulates initiation of digestive enzyme mRNA translation in pancreatic acinar cells and tissue segments in dairy calves25 January 2018 | Bioscience Reports, Vol. 38, No. 1Exocrine PancreasRegulation of Pancreatic SecretionTransport of proteins across membranes — a paradigm in transitionBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, Vol. 1241, No. 3Induction of trypsinogen secretion in herring larvae (Clupea harengus)Marine Biology, Vol. 112, No. 4Nonparallel transport and mechanisms of secretionBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, Vol. 1071, No. 2Effect of phenylalanine on pancreatic amylase secretion in chicks (Gallus domesticus)Comparative Biochemistry and Physiology Part A: Physiology, Vol. 97, No. 4Regulation of Digestive Reactions by the Pancreas1 January 2011Responses of the pancreatic digestive enzyme secretion to various combinations of amino acids and cholecystokinin in chicks (Gallus domesticus)Comparative Biochemistry and Physiology Part A: Physiology, Vol. 93, No. 4Responses of the pancreatic digestive enzyme secretion to amino acids, glucose and cholecystokinin in chicksComparative Biochemistry and Physiology Part A: Physiology, Vol. 92, No. 3Trypsin content in intestines of herring larvae, Clupea harengus, ingesting inert polystyrene spheres or live crustacea preyMarine Biology, Vol. 98, No. 3Variations in the content of trypsin and trysinogen in larval herring (Clupea harengus) digesting copepod naupliiMarine Biology, Vol. 94, No. 2Digestive end products release pancreatic enzymes from particulate cellular pools, particularly zymogen granulesBiochimica et Biophysica Acta (BBA) - General Subjects, Vol. 881, No. 2The Biological Functions and Physiological Effects of Ingested Inhibitors of Digestive ReactionsPancreatic Secretion by Nonparallel Exocytosis: Potential Resolution of a Long ControversyScience, Vol. 228, No. 4702Effects of intravenous infusion of amino acids, fat, or glucose on unstimulated pancreatic secretion in healthy humansDigestive Diseases and Sciences, Vol. 30, No. 5Exocrine pancreas: difference in the amylase content of the dorsal and ventral regionsExperientia, Vol. 39, No. 9Dietary regulation of pancreatic protein synthesisBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, Vol. 654, No. 1Untersuchungen zur Regulation der Gallenblasen-und Pankreastätigkeit des Huhnes9 October 2009 | Zeitschrift für Tierphysiologie Tierernährung und Futtermittelkunde, Vol. 45, No. 1-5Isoelectric focusing studies of human pancreatic secretionJournal of Chromatography B: Biomedical Sciences and Applications, Vol. 221, No. 2Studies on human pure pancreatic juice collected by endoscopic retrograde catheterization of the papillaGastroenterologia Japonica, Vol. 13, No. 5SYNTHESIS, INTRACELLULAR TRANSPORT AND DISCHARGE OF EXPORTABLE PROTEINS IN THE PANCREATIC ACINAR CELL AND OTHER CELLSBiological Reviews, Vol. 53, No. 2La Sécrétion Des Enzymes Digestifs Chez Les Vertébrés: Part 126 September 2008 | Archives Internationales de Physiologie et de Biochimie, Vol. 85, No. 4La Sécrétion Des Enzymes Digestifs Chez Les Vertébrés: Part 226 September 2008 | Archives Internationales de Physiologie et de Biochimie, Vol. 85, No. 4Protein Transport by the PancreasScience, Vol. 190, No. 4216Exocrine Pancreas: Evidence for Topographic Partition of Secretory FunctionScience, Vol. 190, No. 4216Studies on the guinea pig pancreas. Parallel discharge of exocrine enzyme activities.Journal of Biological Chemistry, Vol. 250, No. 7Studies on the pancreas of the guinea pig. Parallel processing and discharge of exocrine proteins.Journal of Biological Chemistry, Vol. 250, No. 7Candidate Hormones of the GutGastroenterology, Vol. 67, No. 4Selective Pancreatic Enzyme Secretion due to a New Peptide Called ChymodeninScience, Vol. 183, No. 4129 More from this issue > Volume 226Issue 1January 1974Pages 77-83 Copyright & PermissionsCopyright © 1974 by American Physiological Societyhttps://doi.org/10.1152/ajplegacy.1974.226.1.77PubMed4809890History Published online 1 January 1974 Published in print 1 January 1974 Metrics

Studies on human pancreatic lipase: I. Interconversion between low and high molecular forms of human pancreatic lipase

Two pancreatic Lipases (glycerol-ester hydrolase, EC 3.1.1.3) of different molecular weight were found in human pancreatic juice. The low molecular weight lipase was found in pure human pancreatic juice and the high molecular weight lipase in human pancreatic juice mixed with bile by gel fiitration on Sephadex G-200 at pH 8.6. The high molecular weight lipase seems very similar to “lipase rapide” reported by Sarda et al.1 in its behavior on gel filtration. Crude and purified high molecular weight lipase was converted to the low molecular weight lipase by extraction with acetone or digestion with phospholipase A. Purified low molecular weight lipase was converted to the high molecular weight form by incubating with pure bile, lecithin or phosphatidylserine but not with lysolecithin nor with sodium taurocholate. The two enzymes were immunologically identical. These results suggest that the high molecular weight lipase exists as a low molecular weight lipase-phospholipid complex. The physiological importance of the conversion of the low molecular weight lipase to its high molecular weight form is discussed.