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Untersuchungen zur biliären Elimination von Enzymen

II. Verhalten von Lactatdehydrogenase, Hydroxybutyratdehydrogenase, Creatin-Phosphokinase, Glutamat-Oxalacetat-Transaminase und Glutamat-Pyruvat-Transaminase

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Zusammenfassung

GOT, GPT, LDH und HbDH finden sich in der menschlichen Lebergalle in Konzentrationen, die den Serumspiegeln entsprechen. Die 24 Std-Ausscheidung beider Transaminasen zeigt ebensogute Korrelation wie die von LDH und HbDH. CPK läßt sich nur sporadisch in der Galle nachweisen. Für die Enzyme GOT, GPT, LDH, Cpl und (teilweise) AP wird eine biliäre Elimination aus dem Serum postuliert, für GlDH, OCT und G-6-PD ist die Leber als ausschließlicher Ursprungsort der biliären Aktivitäten anzusehen.

Summary

GOT, GPT, LDH, and HbDH occur in human bile and serum at equal levels. The daily excretion of GOT versus GPT and LDH versus HbDH shows good correlation. CPK is rarely found in bile. Biliary elimination from serum is claimed for GOT, GPT, LDH, Cpl and AP, whereas liver parenchyma is considered as exclusive source for GlDH, OCT, and G-6-PD in bile.

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Literatur

  1. Allen, H., and M. A. Spellberg: Alkaline phosphatase in bile and urine. Arch. intern. Med.120, 667–671 (1967).

    Google Scholar 

  2. Amelung, D., H. D. Horn u. E. Schröder: Klinische und experimentelle Untersuchungen zur Frage der Ferment-Elimination ausdemSerum. Klin. Wschr.36, 963–970 (1958).

    Google Scholar 

  3. Brighenti, L., C. Ottolenghi, L. Passerini, und O. Barnabei: Acetylcholine control of amylase activity in the isolated perfused rat liver. Biochim. biophys. Acta (Amst.)130, 272–275 (1966).

    Google Scholar 

  4. Bücher, Th., u. D. Pette: Über die Enzymaktivitätsmuster in Bezug zur Differenzierung der Skeletmuskulatur. Dtsch. Ges. Inn. Med., 71. Tagg, 104–124 (1965).

    Google Scholar 

  5. Chenderovitch, J.: Stop-flow analysis of bile secretion. Amer. J. Physiol.214, 86–93 (1968).

    Google Scholar 

  6. Chiandussi, L., S. F. Greene, and S. Sherlock: Serum alkaline phosphatase fractions in hepato-biliary and bone diseases. Clin. Sci.22, 425–434 (1962). Zit. nach 41.

    Google Scholar 

  7. Chinsky, M., and S. Sherry: Serum transaminase as a diagnostic aid. Arch. intern. Med.99, 556–568 (1957).

    Google Scholar 

  8. —— G. L. Shmagranoff, and S. Sherry: Serum transaminase activity. J. Lab. clin. Med.47, 108–118 (1956).

    Google Scholar 

  9. Clubb, J. S., F. C. Neale, and S. Posen: The behaviour of infused human placental alkaline phosphatase in human subjects. J. Lab. clin. Med.66, 493–507 (1965).

    Google Scholar 

  10. Dalgaard, J. B.: Serum and bile phosphatase in biliary fistula dogs. Acta physiol. scand.16, 293–307 (1949). Zit.nach 41.

    Google Scholar 

  11. —— On the cause of increase in serum phosphatase in obstructive jaundice. Acta physiol. scand.22, 200–210 (1951) Zit. nach 9.

    Google Scholar 

  12. Drill, V. A., J. A. Annegers, E. F. Snapp, and A. C. Ivy: Effect of biliary fistula on bromsulphalein retention, serum phosphatase and bile phosphatase. J. clin. Invest.24, 97–105 (1945).

    Google Scholar 

  13. Dunn, M., J. Martins, and K. R. Reissmann: The disappearance rate of glutamic oxalacetic transaminase from the circulation and its distribution in the body's fluid compartments and secretions. J. Lab. clin. Med.51, 259–265 (1958).

    Google Scholar 

  14. Edlund, Y., and E. Christoffersson: Alkaline phosphatase and transaminases in serum and hepatic duct bile in patients with normal or blocked biliary flow. Acta hepatosplenol. (Stuttg.)14, 230–237 (1967).

    Google Scholar 

  15. Ellman, G. L., K. D. Courtney, V. Andres, and R. M. Featherstone: A new and rapid colorimetric determination of acetylcholinesterase. Biochem. Pharmacol.7, 88–95 (1961).

    Google Scholar 

  16. Estborn, B.: Visualization of acid and alkaline phosphatase after starch-gel electrophoresis of seminal plasma, serum and bile. Nature (Lond.)184 (Suppl. 21), 1636–1637 (1959). Zit. nach 41

    Google Scholar 

  17. Flock, E. V., M. A. Block, J. L. Bollmann, and F. C. Mann: Alkaline phosphatase and amylase of plasma after hepatectomy. Amer. J. Physiol.170, 467–471 (1952).

    Google Scholar 

  18. Frankl, H. D., and J. H. Merritt: Enzyme activity in the serum and common duct bile of dogs. Amer. J. Gastroent.31, 166–170 (1959). Zit. nach 14.

    Google Scholar 

  19. Garry, P. J., and J. I. Routh: A micromethod for serum-cholinesterase. Clin. Chem.1, 91–96 (1965).

    Google Scholar 

  20. Gault, M. H., J. Stein, and A. Aronoff: Serum ceruloplasmin in hepatobiliary and other disorders: significance of abnormal values. Gastroenterology50, 8–18 (1966).

    Google Scholar 

  21. Gordon, S.: Alkaline phosphatase isoenzymes in serum and tissue. S. Afr. med. J.39, 49–53 (1965).

    Google Scholar 

  22. Hardwicke, J., K. J. Baker, J. G. Rankin, and R. Preisig: Quantitative analyses on dog and human hepatic bile. Protides of the biological fluids. Proc. 11th Coll., p. 264–268 (1963). Amsterdam: Elsevier 1964.

    Google Scholar 

  23. Igaki, A.: Clinical and experimental studies on serum arginase in hepato-biliary disorders. 1. Serum arginase activities under various experimental conditions. Jap. Arch. intern. Med.11, 1–7 (1964).

    Google Scholar 

  24. Kalow, W., und H. A. Lindsay: Comparison of optical and manometric methods for assay of human serum choline-sterase. Canad. J. Biochem.33, 568–574 (1955).

    Google Scholar 

  25. Keiding, N. R.: The alkaline phosphatase fractions of human lymph. Clin. Sci.26, 291–297 (1964). Zit. nach 41.

    Google Scholar 

  26. Kunitz, M., nach E. Layne: Spectrophotometric and turbidimetric methods for measuring proteins. In: Colowick-Kaplan, Methods in enzymology, vol. III, p. 447. New York: Academic Press 1957.

    Google Scholar 

  27. Le Veen, H. H., L. J. Talbot, M. Restuccia, and J. R. Barberio: Metabolism and excretion of alkaline phosphatase: relation to liver function and determination of maximal secretory rates of liver. J. Lab. clin. Med.36, 192–205 (1950).

    Google Scholar 

  28. Linde, S.: On the mechanism of the elevation of serum glutamic-oxalacetic transaminase in obstructive jaundice. Scand. J. clin. Lab. Invest.10, 308–309 (1958). Zit. nach 14

    Google Scholar 

  29. Lorentz, K.: Aktivitätsbestimmungen von Transaminasen im Duodenalinhalt. Acta hepato-splenol. (Stuttg.)9, 403–408 (1962).

    Google Scholar 

  30. —— Untersuchung von Enzymaktivitäten in der Blasengalle. Klin. Wschr.41, 18–21 (1963).

    Google Scholar 

  31. -- Untersuchungen über Eigenschaften und Herkunft menschlicher Serumamylase. Habil.-Schr. Lübeck 1969.

  32. -- Einfluß von Blasengalle auf die Aktivität von Enzymen Enzymol. biol. clin (im Druck).

  33. ——, J. Adlung: Zur Bestimmung der Ornithin-Carbamyl-Transferase im Serum. Med. Lab.21, 102–108 (1968).

    Google Scholar 

  34. Mahy, B. W. J., K. E. K. Rowson, and C. W. Parr: Studies on the mechanism of action of Riley virus IV. The reticuloendothelial system and impaired plasma enzyme clearance in infected mice. J. exp. Med.125, 277–288 (1967).

    Google Scholar 

  35. Massarrat, S.: Studien über die Schwundrate und Alterung der zugeführten J131-markierten homologen GOT und GPT beim Schwein. Dtsch. Ges. Inn. Med.71, Tagg, 946–949 (1965).

    Google Scholar 

  36. McGeachin, R. L., and B. A. Potter: Amylase synthesis and transport in the isolated, perfused liver. Advances in enzyme regulation, vol.3, p. 137–143. (G. Weber). Oxford: Pergamon Press 1965.

    Google Scholar 

  37. Mezey, E., G. R. Cherrick, and P. R. Holt: Biliary excretion of alcohol dehydrogenase. J. Lab. clin. Med.71, 798–806 (1968).

    Google Scholar 

  38. Miholčič, M., u. B. Večerek: Die Änderungen in den Serum-und Urinisoamylasen bei der Unterbindung des Ductus choledochus der weißen Ratte. Clin. chim. Acta16, 383–388 (1967).

    Google Scholar 

  39. Morrison, G. R.: Hexokinase and glucokinase activities in bile duct epithelial cells and hepatic cells from normal rat and human livers. Arch. Biochem.122, 569–573 (1967).

    Google Scholar 

  40. Pappo, A., et I. Apostolesco: Données actuelles sur l'activité enzymatique de la bile Rev. roum. Méd. interne4, 163–167 (1967).

    Google Scholar 

  41. Peterlik, M.: Bestimmung der Aktivität der alkalischen Phosphatase in der Galle. Z. klin. Chem.4, 34–35 (1966).

    Google Scholar 

  42. Polin, S. G., M. A. Spellberg, L. Teitelman, and M. Okumura: The origin of elevated serum alkaline phosphatase in hepatic disease. Gastroenterology42, 431–438 (1962).

    Google Scholar 

  43. Polonovski, M., et R. Bourillon: Etude sur la composition des biles dans la série animale. Bull. Soc. Chim. biol. (Paris)34, 703–711 (1952).

    Google Scholar 

  44. Pope, C. E., and S. R. Cooperband: Protein characteristics of serum and bile alkaline phosphatase. Gastroenterology,50, 631–636 (1966).

    Google Scholar 

  45. Ravin, H. A.: An improved colorimetric enzymatic assay of ceruloplasmin. J. Lab. clin. Med.58, 161–168 (1961).

    Google Scholar 

  46. Richterich, R.: Klinische Chemie. Frankfurt a. M.: Akademische Verlagsanstalt 1965.

  47. Rick, W., u. T. V. Hausamen: Optisch-kinetischer Test zur Bestimmung der alkalischen Phosphatase. Z. anal. Chem.212, 267–268 (1965).

    Google Scholar 

  48. Schultz, C., u. E. Schmidt: Gallengangsverschluß und Enzymaktivitäten im Serum. Klin. Wschr.45, 162–163 (1967).

    Google Scholar 

  49. Sebesta, D. G., F. J. Bradshaw, and D. J. Prockop: Source of the elevated serum alkaline phosphatase activity in biliary obstruction: studies utilizing isolated liver perfusion. Gastroenterology47, 166–170 (1964).

    Google Scholar 

  50. Sterling, J., and S. Winsten: Enzymes in bile. J. Einstein Med. Cent.7, 112–114 (1959). Zit. nach 41.

    Google Scholar 

  51. Trautschold, I.: Enzyme im Serum bei Herzerkrankungen. Praktische Enzymologie, S. 241. Bern: Huber 1968.

    Google Scholar 

  52. Wakim, K. G., and G. A. Fleischer: 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.61, 86–92 (1963).

    Google Scholar 

  53. Weber, H.: Rasche und einfache Ultramikromethode zur Bestimmung der Serumcholinesterase. Dtsch. med. Wschr.43, 1927–1932 (1966).

    Google Scholar 

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Lorentz, K., Jaspers, G. & Adlung, J. Untersuchungen zur biliären Elimination von Enzymen. Klin Wochenschr 48, 218–220 (1970). https://doi.org/10.1007/BF01485061

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