Ricerca in clinica e in laboratorio

, Volume 5, Issue 2, pp 97–104 | Cite as

The assay of exocrinous peptidases in clinical chemistry

  • Marc Roth


The various peptidases secreted by such exocrine tissues as gastric mucosa, pancreas and prostate are usually determined by catalytic methods. Another approach utilizes immunoassay. Endopeptidases were formerly assayed with protein substrates such as hemoglobin and albumin. These techniques are increasingly replaced by more specific ones using artificial peptide derivatives as substrates, some of which allow an increase in absorbance or fluorescence to be continuously recorded. The presently available methods of assaying pepsin, pancreatic trypsin, trypsinogen and carboxypeptidase A, enterokinase and several peptidases of human sperm are reviewed.


Carboxypeptidases Chymotrypsin Duodenal juice Enterokinase Gastric juice Pancreas Pepsin Peptidases Prostate Sperm Trypsin 


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  1. 1).
    Adham N. F., Dyce B., Haverback B. J.: Trypsin-Binding α2-Macroglobulin in Patients with Acute Pancreatitis — Gastroenterology62, 365, 1972.PubMedGoogle Scholar
  2. 2).
    Appel W.: Carboxypeptidase A — In:Bergmeyer H. U. (Ed.): Methoden der enzymatischen Analyse. 3. Ed., Verlag Chemie, Weinheim, 1974; p. 1030.Google Scholar
  3. 3).
    Bergström K., Lundh G.: Determination of Trypsin in Duodenal Fluid as a Test of Pancreatic Function — Scand. J. Gastroent.5, 533, 1970.PubMedGoogle Scholar
  4. 4).
    Bieth J., Metais P., Warter J.: Activation, Inhibition and Protection of Tryptic andα-Chymotryptic Activity by Normal Human Serum — Clin. chim. Acta20, 69, 1968.PubMedCrossRefGoogle Scholar
  5. 5).
    Borgström B.: Pancreatic Juice and Duodenal Content — In:Curtius H.-C., Roth M. (Eds): Clinical Biochemistry, Principles and Methods. W. de Gruyter, Berlin, 1974; p. 1258.Google Scholar
  6. 6).
    Butin J. W., Graham W. D.: Serum Exopeptidase Activity in Patients with Pancreatic Disease — Gastroenterology40, 669, 1961.Google Scholar
  7. 7).
    Chariot J.: Le pepsinogène sérique chez les gastrectomisés — Vie méd.49, 1357, 1968.Google Scholar
  8. 8).
    Chariot J., Hardouin J. P., Lanfranchi J., Debray Ch.: Détermination du pepsinogène sérique au cours de diverses maladies digestives. Intérêt clinique et physio-pathologique de son dosage — Sem. Hôp. Paris42, 1491, 1966.Google Scholar
  9. 9).
    Choi H. J., Goldstein F., Wirts C. W., Menduke H.: Normal Duodenal Trypsin Values in Response to Secretin-Pancreozymin Stimulation with Preliminary Data in Patients with Pancreatic Disease — Gastroenterology53, 397, 1967.PubMedGoogle Scholar
  10. 10).
    Cushman D. W., Cheung H. S.: concentrations of Angiotensin-Converting Enzyme in Tissues of the Rat — Biochim. biophys. Acta (Amst.)250, 261, 1971.Google Scholar
  11. 11).
    Depierre D., Roth M.: Fluorimetric Determination of Dipeptidyl Carboxypeptidase (Angiotensin-I-Converting Enzyme) — Enzyme19, 65, 1975.PubMedGoogle Scholar
  12. 12).
    Depierre D., Roth M., Meylan J.: Some Properties of the Angiotensin-Converting Enzyme from Human Seminal Plasma — Experientia (Basel)29, 751, 1973.Google Scholar
  13. 13).
    Dreiling D. A., Janowitz H. D.: Exocrine Pancreatic Secretion — Amer. J. Med.21, 98, 1956.PubMedCrossRefGoogle Scholar
  14. 14).
    Erlanger B. F., Edel F., Cooper A. G.: Action of Chymotrypsin on Two New Chromogenic Substrates — Arch. Biochem.115, 206, 1966.PubMedCrossRefGoogle Scholar
  15. 15).
    Erlanger B. F., Kokowsky N., Cohen W.: The Preparation and Properties of Two New Chromogenic Substrates of Trypsin — Arch. Biochem.95, 271, 1961.PubMedCrossRefGoogle Scholar
  16. 16).
    Etherington D. J., Taylor W. H.: The Pepsins of Normal Human Gastric Juice — Biochem. J.113, 663, 1969.PubMedGoogle Scholar
  17. 17).
    Felber J.-P.: Radioimmunoassay of Enzymes — In:Curtius H.-C., Roth M. (Eds): Clinical Biochemistry, Principles and Methods. W. de Gruyter, Berlin, 1974; p. 483.Google Scholar
  18. 18).
    Floch M. H., Groisser V. W.: Serum Proteolytic Enzyme Activity in Pancreatic Disease — New Engl. J. Med.263, 1129, 1960.PubMedGoogle Scholar
  19. 19).
    Gregoire A. T., Moran J. M.: The Enzyme Activity, Protein and Fructose Content of Normal, Oligospermic, Post-Vasectomy, and Infertile Azoospermic Men — Fertil. and Steril.24, 208, 1973.Google Scholar
  20. 20).
    Gullick H. D.: Increased Plasma Proteolytic Activity Due to Arginine Amidase in Patients with Pancreatitis — New Engl. J. Med.268, 851, 1963.PubMedGoogle Scholar
  21. 21).
    Hadorn B.: Diseases of the Pancreas in Children Clinics — Gastroenterology1, 125, 1972.Google Scholar
  22. 22).
    Hadorn B., Tarlow M. J., Lloyd J. K., Wolff O. H.: Intestinal Enterokinase Deficiency — Lancet1, 812, 1969.PubMedCrossRefGoogle Scholar
  23. 23).
    Haverback B. J., Dyce B. J., Bundy H. F., Wirtschafter S. K., Edmondson H. A.: Protein Binding of Pancreatic Proteolytic Enzymes — J. clin. Invest.41, 972, 1962.PubMedCrossRefGoogle Scholar
  24. 24).
    Haverback B. J., Swanson V. L., Rinderknecht H., Wick M., Silverman P., Dyce B. J.: Proteolytic Enzymes and Pancreatitis — In:Beck I. T., Sinclair D. G. (Eds): The Exocrine Pancreas. J. and A. Churchill, London, 1971; p. 121.Google Scholar
  25. 25).
    Hirsch-Marie H.: Dosage immunologique du pepsinogène et de la pepsine gastrique et urinaire par la méthode de Laurell — Clin. chim. Acta24, 411, 1969.PubMedCrossRefGoogle Scholar
  26. 26).
    Hirsch-Marie H., Conte M.: Immunochemical Quantitation of Pepsin and Pepsinogen — Digestion3, 338, 1970.PubMedCrossRefGoogle Scholar
  27. 27).
    Hoar C. S., Browning J. R.: Plasma Pepsinogen in Peptic Ulcer Disease and Other Gastric Disorders — New Engl. J. Med.255, 153, 1956.PubMedGoogle Scholar
  28. 28).
    Huggins C., Vail V. C.: Plasma Coagulation and Fibrinogenolysis by Prostatic Fluid and Trypsin — Amer. J. Physiol.139, 129, 1943.Google Scholar
  29. 29).
    Krampitz G., Doepfmer R.: Über das Vorkommen der Leucineaminopeptidase im menschlichen Spermliquor — Klin. Wschr.39, 1300, 1961.PubMedCrossRefGoogle Scholar
  30. 30).
    Kunitz M.: Formation of Trypsin from Crystalline Trypsinogen by Means of Enterokinase — J. gen. Physiol.22, 429, 1939.CrossRefPubMedGoogle Scholar
  31. 31).
    Louvard D., Maroux S., Baratti J., Desnuelle P.: On the Distribution of Enterokinase in Porcine Intestine and on Its Subcellular Distribution — Biochim. biophys. Acta (Amst.)309, 127, 1973.Google Scholar
  32. 32).
    Lundh G.: Diagnostic Investigation of the External Pancreatic Secretion — In: XXI Congrès de la Société internationale de Chirurgie. Philadelphia 1965; p. 39.Google Scholar
  33. 33).
    Milstone J. H., Goldblatt M. V., Milstone V. K.: Physiologic Fitness of Enterokinase — Proc. Soc. exp. Biol. (N.Y.)131, 1438, 1969.Google Scholar
  34. 34).
    Mirsky I. A., Futterman P., Kaplan S.: Blood Plasma Pepsinogen. II. Activity of Plasma from ‘Normal’ Subjects, Patients with Duodenal Ulcer, and Patients with Pernicious Anemia — J. Lab. clin. Med.40, 188, 1952.PubMedGoogle Scholar
  35. 35).
    Nagel W., Willig T., Peschke W., Schmidt F. H.: Über die Bestimmung von Trypsin und Chymotrypsin mit Aminosäurep-Nitroaniliden — Hoppe-Seylers Z. physiol. Chem.340, 1, 1965.PubMedGoogle Scholar
  36. 36).
    Nordström, C., Dahlquist A.: Rat Enterokinase: The Effect of Ions and Its Localization in the Intestine — Biochim. biophys. Acta (Amst.)242, 209, 1971.Google Scholar
  37. 37).
    Ohlsson K., Tegner H.: Experimental Pancreatitis in the Dog. Demonstration of Trypsin in Ascitic Fluid, Lymph and Plasma — Scand. J. Gastroent.8, 129, 1973.PubMedGoogle Scholar
  38. 38).
    Rasmussen J., Albrechtsen O. K.: Fibrinolytic Activity in Human Seminal Plasma — Fertil. and Steril.11, 264, 1960.Google Scholar
  39. 39).
    Reinharz A., Roth M.: Studies on the Trypsin-Like and the Trypsin-Inhibiting Properties of Human Serum — Enzymol. biol. clin.5, 113, 1965.Google Scholar
  40. 40).
    Rick W.: Zur Bestimmung der Carboxypeptidase im Duodenalsaft — Klin. Wschr.38, 408, 1960.CrossRefGoogle Scholar
  41. 41).
    Rinderknecht H., Engeling E. R., Bunnell M. J., Geokas M. C.: A Sensitive Assay for Human Enterokinase and Some Properties of the Enzyme — Clin. chim. Acta54, 145, 1974.PubMedCrossRefGoogle Scholar
  42. 42).
    Roman W., Favilla I.: The Usefulness of Serum Trypsin Tests — Enzymologia26, 249, 1964.Google Scholar
  43. 43).
    Roth M.: Fluorimetric Assay of Enzymes. VII. Carboxypeptidase A — Meth. biochem. Anal.17, 260, 1969.Google Scholar
  44. 44).
    Samloff I. M.: Immunologic Studies of Human Group I Pepsinogens — J. Immunol.106, 962, 1971.PubMedGoogle Scholar
  45. 45).
    Samloff I. M., Liebman W. M.: Purification and Immunochemical Characterization of Group II Pepsinogens in Human Seminal Fluid — Clin. exp. Immunol.11, 405, 1972.PubMedGoogle Scholar
  46. 46).
    Schill W.-B.: Quantitative Determination of Acrosin Activity in Human Spermatozoa — Fertil. and Steril.25, 703, 1974.Google Scholar
  47. 47).
    Schön H., Rässler B., Henning N.: Über die Untersuchung der exkretorischen Pankreasfunktion. Methoden zur Aktivitätsbestimmung von Trypsin, Chymotrypsin, Carboxypeptidase, Lipase und Diastase — Klin. Wschr.39, 217, 1961.CrossRefGoogle Scholar
  48. 48).
    Shapira E., Arnon R., Russell A.: Specific Immunoassay for Quantitative Determination of Human Trypsin in Intestinal Content — J. Lab. clin. Med.77, 877, 1971.PubMedGoogle Scholar
  49. 49).
    Shapira E., Ben-Yoseph Y., Russell A.: Determination of Trypsin Activity in Human Intestinal Content by Hydrolysis of Benzoyl-DL-Argininep-Nitroanilide — Israel J. med. Sci.6, 670, 1970.PubMedGoogle Scholar
  50. 50).
    Siegelmann A. M., Carlson A. S., Robertson T.: Investigation of Serum Trypsin and Related Substances. I. The Qualitative Demonstration of Trypsin-Like Activity in Human Blood Serum by a Micromethod — Arch. Biochem.97, 159, 1962.CrossRefGoogle Scholar
  51. 51).
    Sievers M. L., Fischer G. L.: Indirect Gastric Secretory Studies. A Comparison of Tubeless Gastric Analysis and Plasma Pepsinogen Determination as Screening Procedures — Amer. J. dig. Dis.2, 363, 1957.PubMedCrossRefGoogle Scholar
  52. 52).
    Singh A. K., Shinton N. K.: Serum Pepsinogen in the Differentiation of Megaloblastic Anaemia — J. clin. Path.18, 349, 1965.PubMedCrossRefGoogle Scholar
  53. 53).
    Spiro H. M., Ryan A. E., Jones C. M.: The Relation of Blood Pepsin to Gastric Secretion with Particular Reference to Anacidity and Achylia — Gastroenterology30, 563, 1956.PubMedGoogle Scholar
  54. 54).
    Szczeklik A.: Trypsin-Like Activity of Serum: Its Origin and Electrophoretic Separation — Clin. chim. Acta23, 219, 1969.PubMedCrossRefGoogle Scholar
  55. 55).
    Szczeklik E., Orlowski M., Szczeklik A., Narczewska B.: The Activity of Plasma, Serum, Thrombin, and Plasmin toward Synthetic Trypsin Substrates — Thrombos. Diathes. haemorrh. (Stuttg.)19, 99, 1968.Google Scholar
  56. 56).
    Tagnon H. J., Schulman P., Whitmore W. F., Leone L. A.: Prostatic Fibrinolysin: Study of a Case Illustrating Role in Hemorrhagic Diathesis of Cancer of the Prostate — Amer. J. Med.15, 875, 1953.PubMedCrossRefGoogle Scholar
  57. 57).
    Taylor W. H.: Pepsins of Patients of with Peptic Ulcer — Nature (Lond.)227, 76, 1970.CrossRefGoogle Scholar
  58. 58).
    Whitecross D. P., Armstrong C., Clarke A. D., Piper D. W.: The Pepsinogens of Human Gastric Mucosa — Gut14, 850, 1973.PubMedCrossRefGoogle Scholar
  59. 59).
    Wormsley K. G.: Further Studies of the Response to Secretin and Pancreozymin in Man — Scand. J. Gastroent.6, 343, 1971.PubMedCrossRefGoogle Scholar
  60. 60).
    Ying S. H., Day E., Whitmore W. F., Tagnon H. J.: Fibrinolytic Activity in Human Prostatic Fluid and Semen — Fertil. and Steril.7, 80, 1956.Google Scholar
  61. 61).
    Zaneveld L. J. D., Schumacher G. F. B., Travis J.: Human Sperm Acrosomal Proteinase: Antibody Inhibition and Immunologic Dissimilarity to Human Pancreatic Trypsin — Fertil. and Steril.24, 479, 1973.Google Scholar

Copyright information

© Springer-Verlag 1975

Authors and Affiliations

  • Marc Roth
    • 1
  1. 1.Laboratoire CentralHôpital CantonalGenève 4Switzerland

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