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.
Literatur
Allen, H., and M. A. Spellberg: Alkaline phosphatase in bile and urine. Arch. intern. Med.120, 667–671 (1967).
Amelung, D., H. D. Horn u. E. Schröder: Klinische und experimentelle Untersuchungen zur Frage der Ferment-Elimination ausdemSerum. Klin. Wschr.36, 963–970 (1958).
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).
Bücher, Th., u. D. Pette: Über die Enzymaktivitätsmuster in Bezug zur Differenzierung der Skeletmuskulatur. Dtsch. Ges. Inn. Med., 71. Tagg, 104–124 (1965).
Chenderovitch, J.: Stop-flow analysis of bile secretion. Amer. J. Physiol.214, 86–93 (1968).
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.
Chinsky, M., and S. Sherry: Serum transaminase as a diagnostic aid. Arch. intern. Med.99, 556–568 (1957).
—— G. L. Shmagranoff, and S. Sherry: Serum transaminase activity. J. Lab. clin. Med.47, 108–118 (1956).
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).
Dalgaard, J. B.: Serum and bile phosphatase in biliary fistula dogs. Acta physiol. scand.16, 293–307 (1949). Zit.nach 41.
—— On the cause of increase in serum phosphatase in obstructive jaundice. Acta physiol. scand.22, 200–210 (1951) Zit. nach 9.
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).
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).
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).
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).
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
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).
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.
Garry, P. J., and J. I. Routh: A micromethod for serum-cholinesterase. Clin. Chem.1, 91–96 (1965).
Gault, M. H., J. Stein, and A. Aronoff: Serum ceruloplasmin in hepatobiliary and other disorders: significance of abnormal values. Gastroenterology50, 8–18 (1966).
Gordon, S.: Alkaline phosphatase isoenzymes in serum and tissue. S. Afr. med. J.39, 49–53 (1965).
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.
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).
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).
Keiding, N. R.: The alkaline phosphatase fractions of human lymph. Clin. Sci.26, 291–297 (1964). Zit. nach 41.
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.
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).
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
Lorentz, K.: Aktivitätsbestimmungen von Transaminasen im Duodenalinhalt. Acta hepato-splenol. (Stuttg.)9, 403–408 (1962).
—— Untersuchung von Enzymaktivitäten in der Blasengalle. Klin. Wschr.41, 18–21 (1963).
-- Untersuchungen über Eigenschaften und Herkunft menschlicher Serumamylase. Habil.-Schr. Lübeck 1969.
-- Einfluß von Blasengalle auf die Aktivität von Enzymen Enzymol. biol. clin (im Druck).
——, J. Adlung: Zur Bestimmung der Ornithin-Carbamyl-Transferase im Serum. Med. Lab.21, 102–108 (1968).
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).
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).
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.
Mezey, E., G. R. Cherrick, and P. R. Holt: Biliary excretion of alcohol dehydrogenase. J. Lab. clin. Med.71, 798–806 (1968).
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).
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).
Pappo, A., et I. Apostolesco: Données actuelles sur l'activité enzymatique de la bile Rev. roum. Méd. interne4, 163–167 (1967).
Peterlik, M.: Bestimmung der Aktivität der alkalischen Phosphatase in der Galle. Z. klin. Chem.4, 34–35 (1966).
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).
Polonovski, M., et R. Bourillon: Etude sur la composition des biles dans la série animale. Bull. Soc. Chim. biol. (Paris)34, 703–711 (1952).
Pope, C. E., and S. R. Cooperband: Protein characteristics of serum and bile alkaline phosphatase. Gastroenterology,50, 631–636 (1966).
Ravin, H. A.: An improved colorimetric enzymatic assay of ceruloplasmin. J. Lab. clin. Med.58, 161–168 (1961).
Richterich, R.: Klinische Chemie. Frankfurt a. M.: Akademische Verlagsanstalt 1965.
Rick, W., u. T. V. Hausamen: Optisch-kinetischer Test zur Bestimmung der alkalischen Phosphatase. Z. anal. Chem.212, 267–268 (1965).
Schultz, C., u. E. Schmidt: Gallengangsverschluß und Enzymaktivitäten im Serum. Klin. Wschr.45, 162–163 (1967).
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).
Sterling, J., and S. Winsten: Enzymes in bile. J. Einstein Med. Cent.7, 112–114 (1959). Zit. nach 41.
Trautschold, I.: Enzyme im Serum bei Herzerkrankungen. Praktische Enzymologie, S. 241. Bern: Huber 1968.
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).
Weber, H.: Rasche und einfache Ultramikromethode zur Bestimmung der Serumcholinesterase. Dtsch. med. Wschr.43, 1927–1932 (1966).
Author information
Authors and Affiliations
Additional information
Mit Unterstützung der Deutschen Forschungsgemeinschaft.
Rights and permissions
About this article
Cite this article
Lorentz, K., Jaspers, G. & Adlung, J. Untersuchungen zur biliären Elimination von Enzymen. Klin Wochenschr 48, 218–220 (1970). https://doi.org/10.1007/BF01485061
Issue Date:
DOI: https://doi.org/10.1007/BF01485061