Skip to main content
Gut logoLink to Gut
. 1980 Jul;21(7):580–586. doi: 10.1136/gut.21.7.580

Metabolism of 125I-labelled trypsin in man: evidence of recirculation.

G Lake-Bakaar, C E Rubio, S McKavanagh, B J Potter, J A Summerfield
PMCID: PMC1419902  PMID: 7429320

Abstract

125I-labelled human trypsin metabolism has been investigated in man. Three subjects received 125I-trypsin and 131I-albumin intravenously. Against a background secretin infusion (1 U/kg/h), trypsin decayed biexponentially from the serum with half-lives of 17.5, 21, and 24 minutes for the rapid disappearance phase and 520, 540, and 560 minutes for the slow phase. Between 13% and 38% of the 125I injected was recovered from duodenal juice aspirated continously over 300 minutes. In contrast, less than 1% of the 131I-albumin injected was recovered. When bile and pure pancreatic juice were collected at endoscopic retrograde cholangiopancreatography after intravenous 125I-trypsin in a fourth subject 125I radioactivity was found to be secreted via both these routes. After 125I-trypsin infusion into the duodenum 11% of the total dose was found to be present in the circulation after 75 minutes. These results support the concept that recirculation of trypsin exists in man.

Full text

PDF
580

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. AVAKIAN S. FURTHER STUDIES ON THE ABSORPTION OF CHYMOTRYPSIN. Clin Pharmacol Ther. 1964 Nov-Dec;5:712–715. doi: 10.1002/cpt196456part1712. [DOI] [PubMed] [Google Scholar]
  2. Borgström A., Ohlsson K. Studies on the turnover of endogenous cathodal trypsinogen in man. Eur J Clin Invest. 1978 Dec;8(6):379–382. doi: 10.1111/j.1365-2362.1978.tb00868.x. [DOI] [PubMed] [Google Scholar]
  3. Donaldson L. A., Joffe S. N., McIntosh W., Brodie M. J. Amylase activity in human bile. Gut. 1979 Mar;20(3):216–218. doi: 10.1136/gut.20.3.216. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Elias E., Redshaw M., Wood T. Diagnostic importance of changes in circulating concentrations of immunoreactive trypsin. Lancet. 1977 Jul 9;2(8028):66–68. doi: 10.1016/s0140-6736(77)90066-6. [DOI] [PubMed] [Google Scholar]
  5. GITIL D., LANDING B. H., WHIPPLE A. The localization of homolgous plasma proteins in the tissues of young human beings as demonstrated with fluorescent antibodies. J Exp Med. 1953 Feb 1;97(2):163–176. doi: 10.1084/jem.97.2.163. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. GOLDSMITH R. E., STEVENS C. D., SCHIFF L. Concentration of iodine in the human stomach and other tissues as determined with radioactive iodine. J Lab Clin Med. 1950 Apr;35(4):497–503. [PubMed] [Google Scholar]
  7. Goldberg D. M., Campbell R., Roy A. D. Binding of trypsin and chymotrypsin by human intestinal mucosa. Biochim Biophys Acta. 1968 Nov 19;167(3):613–615. doi: 10.1016/0005-2744(68)90053-3. [DOI] [PubMed] [Google Scholar]
  8. Götze H., Rothman S. S. Enteropancreatic circulation of digestive enzyme as a conservation mechanism. Nature. 1975 Oct 16;257(5527):607–609. doi: 10.1038/257607a0. [DOI] [PubMed] [Google Scholar]
  9. KABACOFF B. L., WOHLMAN A., UMHEY M., AVAKIAN S. ABSORPTION OF CHYMOTRYPSIN FROM THE INTESTINAL TRACT. Nature. 1963 Aug 24;199:815–815. doi: 10.1038/199815a0. [DOI] [PubMed] [Google Scholar]
  10. Katayama K., Fujita T. Studies on biotransformation of elastase. I. Transport of 131 I-labeled elastase across rat intestine in vitro. Biochim Biophys Acta. 1972 Oct 23;288(1):172–180. doi: 10.1016/0005-2736(72)90235-0. [DOI] [PubMed] [Google Scholar]
  11. Katayama K., Fujita T. Studies on biotransformation of elastase. II. Intestinal absorption of 131 I-labelled elastase in vivo. Biochim Biophys Acta. 1972 Oct 23;288(1):181–189. doi: 10.1016/0005-2736(72)90236-2. [DOI] [PubMed] [Google Scholar]
  12. LaBadie J. H., Chapman K. P., Aronson N. N., Jr Glycoprotein catabolism in rat liver: Lysosomal digestion of iodinated asialo-fetuin. Biochem J. 1975 Nov;152(2):271–279. doi: 10.1042/bj1520271. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Leibow C., Rothman S. S. Enteropancreatic circulation of digestive enzymes. Science. 1975 Aug 8;189(4201):472–474. doi: 10.1126/science.1154022. [DOI] [PubMed] [Google Scholar]
  14. MARTIN G. J., BOGNER R. L., EDELMAN A. Further in vivo observations with radioactive trypsin. Am J Pharm Sci Support Public Health. 1957 Nov;129(11):386–392. [PubMed] [Google Scholar]
  15. MATTHEWS C. M. The theory of tracer experiments with 131I-labelled plasma proteins. Phys Med Biol. 1957 Jul;2(1):36–53. doi: 10.1088/0031-9155/2/1/305. [DOI] [PubMed] [Google Scholar]
  16. MEGEL H., STRAUSS R., HO R., BEILER M. DETECTION OF TRYPSIN-LIKE ACTIVITY IN THE PLASMA OF RATS AFTER ORAL ADMINISTRATION OF TRYPSIN. Arch Biochem Biophys. 1964 Nov;108:193–199. doi: 10.1016/0003-9861(64)90375-3. [DOI] [PubMed] [Google Scholar]
  17. MILLER J. M., WILLIARD R. F., POLACHEK A. A. An investigation of trypsin I-131 in patients. Exp Med Surg. 1960;18:352–370. [PubMed] [Google Scholar]
  18. McConahey P. J., Dixon F. J. A method of trace iodination of proteins for immunologic studies. Int Arch Allergy Appl Immunol. 1966;29(2):185–189. doi: 10.1159/000229699. [DOI] [PubMed] [Google Scholar]
  19. McFarlane A. S., Koj A. Short-term measurement of catabolic rates using iodine-labeled plasma protein. J Clin Invest. 1970 Oct;49(10):1903–1911. doi: 10.1172/JCI106409. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. REISFELD R. A., LEWIS U. J., WILLIAMS D. E. Disk electrophoresis of basic proteins and peptides on polyacrylamide gels. Nature. 1962 Jul 21;195:281–283. doi: 10.1038/195281a0. [DOI] [PubMed] [Google Scholar]
  21. Robberecht P., Cremer M., Christophe J. Discharge of newly synthesized proteins in pure juice collected from the human pancreas. Indication of more than one pool of intracellular digestive enzymes. Gastroenterology. 1977 Mar;72(3):417–420. [PubMed] [Google Scholar]
  22. Robberecht P., Cremer M., Vandermeers A., Vandermeers-Piret M. C., Cotton P., De Neef P., Christophe J. Pancreatic secretion of total protein and of three hydrolases collected in healthy subjects via duodenoscopic cannulation. Effects of secretin, pancreozymin, and caerulein. Gastroenterology. 1975 Aug;69(2):374–379. [PubMed] [Google Scholar]
  23. Saunders J. H., Masoero G., Wormsley K. G. Effect of diazepam and hyoscine butylbromide on response to secretin and cholecystokinin-pancreozymin in man. Gut. 1976 May;17(5):351–353. doi: 10.1136/gut.17.5.351. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Temler R. S., Kägi J. H. Isolation of human trypsin by affinity chromatography. Enzyme. 1977;22(4):249–255. [PubMed] [Google Scholar]
  25. Walker W. A., Isselbacher K. J. Uptake and transport of macromolecules by the intestine. Possible role in clinical disorders. Gastroenterology. 1974 Sep;67(3):531–550. [PubMed] [Google Scholar]
  26. Welsh J. D., Preiser H., Woodley J. F., Crane R. K. An enriched microvillus membrane preparation from frozen specimens of human small intestine. Gastroenterology. 1972 Apr;62(4):572–582. [PubMed] [Google Scholar]

Articles from Gut are provided here courtesy of BMJ Publishing Group

RESOURCES