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. 1971 Jan;50(1):156–165. doi: 10.1172/JCI106469

Distribution, turnover, and mechanism of renal excretion of amylase in the baboon

William C Duane 1,2, Roger Frerichs 1,2, Michael D Levitt 1,2
PMCID: PMC291903  PMID: 5543873

Abstract

Pure amylase was isolated from pancreata and parotid glands of the baboon, an animal which has a serum amylase level and renal clearance of amylase (CAm) similar to man. After bolus injection, both pancreatic and salivary amylase rapidly disappeared from the serum in a monoexponential fashion with a mean serum half-time of approximately 83 min. Only about 24% of the amylase cleared from the serum appeared in the urine indicating that the majority of amylase was removed from the serum by an extraurinary mechanism. The CAm by the kidney was constant over a wide range of serum amylase levels and the ratio of CAm/CIn, which averaged 3.0%, was not influenced by mannitol diuresis. This suggests that the renal excretion of amylase results from glomerular filtration without appreciable tubular reabsorption. Pancreatic amylase was consistently cleared more rapidly by the kidney than was the baboon's endogenous amylase while salivary amylase was consistently cleared less rapidly than endogenous amylase.

The findings in this study provide insight into several of the following clinically observed phenomena: (a) the short serum half-time of amylase accounts for the transient nature of serum amylase elevations in pancreatitis; (b) the extra-urinary removal of amylase accounts for the maintenance of relatively normal amylase levels in uremia; and (c) the more rapid renal clearance of pancreatic amylase compared to salivary amylase may explain the disproportionate elevation of the urinary amylase excretion rate relative to the serum amylase level in acute pancreatitis.

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Selected References

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

  1. Appert H. E., Dimbiloglu M., Pairent F. W., Howard J. M. The disappearance of intravenously injected pancreatic enzymes. Surg Gynecol Obstet. 1968 Dec;127(6):1281–1287. [PubMed] [Google Scholar]
  2. Aw S. E. Separation of urinary isoamylases on cellulose acetate. Nature. 1966 Jan 15;209(5020):298–300. doi: 10.1038/209298b0. [DOI] [PubMed] [Google Scholar]
  3. BERSON S. A., YALOW R. S. Distribution and metabolism of I131 labeled proteins in man. Fed Proc. 1957 Jul;16(2):suppl–18. [PubMed] [Google Scholar]
  4. BERSON S. A., YALOW R. S., SCHREIBER S. S., POST J. Tracer experiments with I131 labeled human serum albumin: distribution and degradation studies. J Clin Invest. 1953 Aug;32(8):746–768. doi: 10.1172/JCI102789. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bergeron M., Morel F. Amino acid transport in rat renal tubules. Am J Physiol. 1969 May;216(5):1139–1149. doi: 10.1152/ajplegacy.1969.216.5.1139. [DOI] [PubMed] [Google Scholar]
  6. Berk J. E. Serum amylase and lipase. Newer perspectives. JAMA. 1967 Jan 9;199(2):98–102. [PubMed] [Google Scholar]
  7. Blainey J. D., Northam B. E. Amylase excretion by the human kidney. Clin Sci. 1967 Jun;32(3):377–383. [PubMed] [Google Scholar]
  8. Boyd J. W. The rates of disappearance of L-lactate dehydrogenase isoenzymes from plasma. Biochim Biophys Acta. 1967 Mar 15;132(2):221–231. doi: 10.1016/0005-2744(67)90141-6. [DOI] [PubMed] [Google Scholar]
  9. Cameron D. P., Burger H. G., Catt K. J., Doig A. Metabolic clearance rate of radioiodinated human growth hormone in man. J Clin Invest. 1969 Sep;48(9):1600–1608. doi: 10.1172/JCI106125. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Chamberlain M. J., Stimmler L. The renal handling of insulin. J Clin Invest. 1967 Jun;46(6):911–919. doi: 10.1172/JCI105597. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Clubb J. S., Neale F. C., Posen S. The behavior of infused human placental alkaline phosphatase in human subjects. J Lab Clin Med. 1965 Sep;66(3):493–507. [PubMed] [Google Scholar]
  12. Dawson D. M., Alper C. A., Seidman J., Mendelsohn J. Measurement of serum enzyme turnover rates. Ann Intern Med. 1969 Apr;70(4):799–805. doi: 10.7326/0003-4819-70-4-799. [DOI] [PubMed] [Google Scholar]
  13. Eto K., Pairent F. W., Appert H. E., Howard J. M. Renal excretion of amylase and lipase by dogs. Arch Surg. 1969 Feb;98(2):241–244. doi: 10.1001/archsurg.1969.01340080133031. [DOI] [PubMed] [Google Scholar]
  14. FLEISHER G. A., WAKIM K. G. The fate of enzymes in body fluids-an experimental study. I. Disappearance rates of glutamic-pyruvic transaminase under various conditions. J Lab Clin Med. 1963 Jan;61:76–85. [PubMed] [Google Scholar]
  15. GROSS J. B., PARKIN T. W., MAHER F. T., POWER M. H. Serum amylase and lipase values in renal and extrarenal azotemia. Gastroenterology. 1960 Jul;39:76–82. [PubMed] [Google Scholar]
  16. HARGAN L. A., MCGEACHIN R. L. Renal clearance of amylase in man. J Appl Physiol. 1956 Jul;9(1):129–131. doi: 10.1152/jappl.1956.9.1.129. [DOI] [PubMed] [Google Scholar]
  17. Hiatt N., Bonorris G., Coverdale G. M., Lanchantin G. F. Hepatic deposition of 131-I labeled amylase in dogs: comparison of enzymatic and isotope measurements. Proc Soc Exp Biol Med. 1968 May;128(1):125–130. doi: 10.3181/00379727-128-32959. [DOI] [PubMed] [Google Scholar]
  18. Hiatt N., Bonorris G., Lanchantin G. F. Influence of reticuloendothelial blockade on the binding of amylase to blood cells. Am J Physiol. 1967 Sep;213(3):744–748. doi: 10.1152/ajplegacy.1967.213.3.744. [DOI] [PubMed] [Google Scholar]
  19. Hiatt N. Hypoglycaemia, elevated liver glycogen and diminished liver amylase in pancreatectomized-enterectomized dogs. Nature. 1966 Apr 23;210(5034):423–424. doi: 10.1038/210423a0. [DOI] [PubMed] [Google Scholar]
  20. Joseph R. R., Olivero E., Ressler N. Electrophoretic study of human isoamylases. A new saccharogenic staining method and preliminary results. Gastroenterology. 1966 Sep;51(3):377–382. [PubMed] [Google Scholar]
  21. KATZ J., ROSENFELD S., SELLERS A. L. Sites of plasma albumin catabolism in the rat. Am J Physiol. 1961 Jun;200:1301–1306. doi: 10.1152/ajplegacy.1961.200.6.1301. [DOI] [PubMed] [Google Scholar]
  22. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  23. LOYTER A., SCHRAMM M. The glycogen-amylase complex as a means of obtaining highly purified alpha-amylases. Biochim Biophys Acta. 1962 Dec 4;65:200–206. doi: 10.1016/0006-3002(62)91039-9. [DOI] [PubMed] [Google Scholar]
  24. Levitt M. D., Rapoport M., Cooperband S. R. The renal clearance of amylase in renal insufficiency, acute pancreatitis, and macroamylasemia. Ann Intern Med. 1969 Nov;71(5):919–925. doi: 10.7326/0003-4819-71-5-919. [DOI] [PubMed] [Google Scholar]
  25. Loyter A., Schramm M. Multimolecular complexes of alpha-amylase with glycogen limit dextrin. Number of binding sites of the enzyme and size of the complexes. J Biol Chem. 1966 Jun 10;241(11):2611–2617. [PubMed] [Google Scholar]
  26. 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]
  27. MCGEACHIN R. L., HARGAN L. A. Amylase clearance and excretion during water diuresis. Proc Soc Exp Biol Med. 1957 Jun;95(2):341–343. doi: 10.3181/00379727-95-23213. [DOI] [PubMed] [Google Scholar]
  28. MILLER F., PALADE G. E. LYTIC ACTIVITIES IN RENAL PROTEIN ABSORPTION DROPLETS. AN ELECTRON MICROSCOPICAL CYTOCHEMICAL STUDY. J Cell Biol. 1964 Dec;23:519–552. doi: 10.1083/jcb.23.3.519. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Maunsbach A. B. Absorption of I-125-labeled homologous albumin by rat kidney proximal tubule cells. A study of microperfused single proximal tubules by electron microscopic autoradiography and histochemistry. J Ultrastruct Res. 1966 Jun;15(3):197–241. doi: 10.1016/s0022-5320(66)80108-9. [DOI] [PubMed] [Google Scholar]
  30. Mulhausen R., Brown D. C., Onstad G. Renal clearance of amylase during pancreatitis. Metabolism. 1969 Aug;18(8):669–674. doi: 10.1016/0026-0495(69)90080-8. [DOI] [PubMed] [Google Scholar]
  31. Mutzbauer H., Schulz G. V. Die Bestimmung der molekularen Konstanten von alpha-Amylase aus Humanspeichel. Biochim Biophys Acta. 1965 Jul 22;102(2):526–532. [PubMed] [Google Scholar]
  32. Mutzbauer H., Schulz G. V. Die Bestimmung der molekularen Konstanten von alpha-Amylase aus Humanspeichel. Biochim Biophys Acta. 1965 Jul 22;102(2):526–532. [PubMed] [Google Scholar]
  33. STEINBERG D., VAUGHAN M. Observations on intracellular protein catabolism studied in vitro. Arch Biochem Biophys. 1956 Nov;65(1):93–105. doi: 10.1016/0003-9861(56)90180-1. [DOI] [PubMed] [Google Scholar]
  34. Seely J. F., Dirks J. H. Micropuncture study of hypertonic mannitol diuresis in the proximal and distal tubule of the dog kidney. J Clin Invest. 1969 Dec;48(12):2330–2340. doi: 10.1172/JCI106199. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Soll A. H. A new approach to molecular configuration applied to aqueous pore transport. J Gen Physiol. 1967 Dec;50(11):2565–2578. doi: 10.1085/jgp.50.11.2565. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. THEODOR E., BIRNBAUM D. THE EFFECT OF DILUTION ON THE ACTIVITY OF AMYLASE AND ITS RELATION TO THE EFFECT OF ELECTROPHORESIS. J Lab Clin Med. 1964 May;63:879–884. [PubMed] [Google Scholar]
  37. UJIHIRA I., SEARCY R. L., BERK J. E., HAYASHI S. A SACCHAROGENIC METHOD FOR ESTIMATING ELECTROPHORETIC AND CHROMATOGRAPHIC DISTRIBUTION OF HUMAN SERUM AMYLASE. Clin Chem. 1965 Feb;11:97–112. [PubMed] [Google Scholar]
  38. WAKIM K. G., FLEISHER G. A. The fate of enzymes in body fluids--an experimental study. II. Disappearance rates of glutamic-oxalacetic transaminase I under various conditions. J Lab Clin Med. 1963 Jan;61:86–97. [PubMed] [Google Scholar]
  39. WAKIM K. G., FLEISHER G. A. The fate of enzymes in body fluids--an experimental study. IV. Relationship of the reticuloendothelial system to activities and disappearance rates of various enzymes. J Lab Clin Med. 1963 Jan;61:107–119. [PubMed] [Google Scholar]
  40. WILDING P. USE OF GEL FILTRATION IN THE STUDY OF HUMAN AMYLASE. Clin Chim Acta. 1963 Nov;8:918–924. doi: 10.1016/0009-8981(63)90016-0. [DOI] [PubMed] [Google Scholar]
  41. Yacoub R. S., Appert H. E., Howard J. M. Metabolism of pancreatic amylase and lipase infused intravenously into dogs. Arch Surg. 1969 Jul;99(1):54–58. doi: 10.1001/archsurg.1969.01340130056010. [DOI] [PubMed] [Google Scholar]

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