DISCHARGE OF NEWLY SYNTHESIZED PROTEINS IN PURE JUICE COLLECTED FROM HUMAN PANCREAS - INDICATION OF MORE THAN ONE POOL OF INTRACELLULAR DIGESTIVE ENZYMES
- 1 January 1977
- journal article
- research article
- Vol. 72 (3) , 417-420
Abstract
The pancreatic secretion of 6 normal human volunteers was collected by endoscopic cannulation of the main pancreatic duct. The appearance of newly synthesized proteins was monitored at 1 min intervals after labeling with [75Se]methionine. The minimum transit time of these proteins from their site of synthesis to the acinar lumen was 36 .+-. 8 min. Stimulation of protein secretion by a rapid i.v. injection of caerulein (40 ng/kg), 1 h after [75Se]methionine administration, greatly decreased (by 73% on an average) the specific radioactivity of the discharged proteins. The concept of a functional heterogeneity of proteins secreted by the human pancreas was supported.This publication has 7 references indexed in Scilit:
- The Action of Secretin on the Secretion of Enzymes by the Human PancreasScandinavian Journal of Gastroenterology, 1968
- RESPONSE TO SECRETIN IN MAN1968
- INTRACELLULAR TRANSPORT OF SECRETORY PROTEINS IN THE PANCREATIC EXOCRINE CELLThe Journal of cell biology, 1967
- Electrolyte secretion from rabbit pancreas in vitroAmerican Journal of Physiology-Legacy Content, 1965
- Action of secretin on pancreatic secretionAmerican Journal of Physiology-Legacy Content, 1961
- Biosynthesis by Escherichia coli of active altered proteins containing selenium instead of sulfurBiochimica et Biophysica Acta, 1957
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951