, Volume 38, Issue 1, pp 43–56 | Cite as

Possible precursors of aminopeptidase and alkaline phosphatase in the proximal tubules of kidney and the crypts of small intestine of mice

  • E. D. Wachsmuth
  • A. Torhorst


Two hydrolytically inactive proteins, one having common antigenic determinants with aminopeptidase and the other with alkaline phosphatase, have been localised in the apical cytoplasm of crypt cells of small intestine and in the cytoplasm of proximal convoluted tubules. In addition, the two proteins are also differently heat labil. Although they could not be detected with mere histochemical stain methods, they were detected by the immunofluorescence sandwich technique using specific antibody directed against either of the solubilised enzymes. The findings were confirmed using the previously described immunohistochemical method (Wachsmuth, 1973). The cellular and subcellular localisation implies that these two proteins are precursors of the hydrolytically active brush border membrane enzymes.


Alkaline Phosphatase Small Intestine Proximal Tubule Brush Border Brush Border Membrane 
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  1. Doell, R., Rosen, G., Kretschmer, N.: Immunochemical studies of intestinal disaccharidases during normal and precocious development. Proc. nat. Acad. Sci. (Wash.) 54, 1268–1273 (1965)Google Scholar
  2. Goldfischer, S., Essner, E., Novikoff, A. B.: The localisation of phosphatase activities at the level of ultrastructure. J. Histochem. Cytochem. 12, 71–95 (1964)Google Scholar
  3. Hugon, J. S., Borgers, M.: Ultrastructural differentiation and enzymatic localisation of phosphatases in the developing duodenal epithelium of the mouse. Histochemie 19, 13–30 (1969)Google Scholar
  4. Leblond, C. P., Messier, P.: Renewal of chief cells and goblet cells in the small intestine as shown by radio-autography after injection of thymidine-H3 into mice. Anat. Rec. 132, 247–260 (1958)Google Scholar
  5. Luz, A., Gössner, W.: The alkaline phosphatase in the small intestine of the mouse during radiation induced atrophy of the villi. Beitr. Path. 148, 180–198 (1973)Google Scholar
  6. Moog, F., Grey, R. D.: Spatial and temporal differentiation of alkaline phosphatase on the intestinal villi of the mouse. J. Cell Biol. 32, C1-C5 (1967)Google Scholar
  7. Morton, R. K.: The purification of alkaline phosphatases of animal tissues. Biochem. J. 57, 595–603 (1954)Google Scholar
  8. Nachlas, M. M., Friedman, M. M., Seligman, A. M.: New observations revealing current misconceptions in the localisation of leucine aminopeptidase. J. Histochem. Cytochem. 9, 608 (1961)Google Scholar
  9. Nachlas, M. M., Monis, B., Rosenblatt, D., Seligman, A. M.: Improvement of the histochemical localisation of leucine aminopeptidase with a new substrate, L-leucyl-4-methoxy-2-naphthylamide. J. biochem. biophys. Cytol. 7, 261–264 (1960)Google Scholar
  10. Nordström, C., Dahlquist, A., Joseffson, L.: Quantitative determination of enzymes in different parts of the villi and crypts of rat small intestine. J. Histochem. Cytochem. 15, 713–721 (1968)Google Scholar
  11. Padykula, H. A.: Recent functional interpretations of intestinal morphology. Fed. Proc. 21, 873–879 (1962)Google Scholar
  12. Padykula, H. A., Strauss, E. W., Ladman, A. J., Gardner, F. H.: A morphologic and histochemical analysis of the human jejunal epithelium in non-tropical sprue. Gastroenterology 40, 735–765 (1961)Google Scholar
  13. Porter, R. R.: The hydrolysis of rabbit γ-globulin and antibodies with crystalline papain. Biochem. J. 73, 119–126 (1959)Google Scholar
  14. Wachsmuth, E. D.: Lokalisation von Aminopeptidase in Gewebeschnitten mit einer neuen Immunfluoreszenztechnik. Histochemie 14, 282–296 (1968)Google Scholar
  15. Wachsmuth, E. D.: An immuno-histochemical method for localisation of enzymes in tissue sections: the use of antibody bound to tissue antigen and its property of binding cross-reactive soluble antigen. Histochemie 37, 251–263 (1973)Google Scholar
  16. Wachsmuth, E. D., Fritze, I., Pfleiderer, G.: An aminopeptidase occurring in pig kidney. I. An improved method of preparation, physical and enzymic properties. Biochemistry 5, 169–174 (1966)Google Scholar
  17. Wachsmuth, E. D., Lachman, P. J.: The use of antigen-antibody precipitate for specific detection of antigens in tissue sections. Immunology 17, 469–479 (1969)Google Scholar
  18. Wachsmuth, E. D., Torhorst, A.: Biogenesis of brush border membranes: alkaline phosphatase and aminopeptidase and their possible precursor proteins after X-ray irradiation of small intestine of C3H mice. Beitr. Path. in pressGoogle Scholar
  19. Webster, H. L., Harrison, D. D.: Enzymatic activities during the transformation of crypt to columnar intestinal cells. Exp. Cell Res. 56, 245–253 (1969)Google Scholar
  20. Weichselbaum, T. E.: An accurate and rapid method for the determination of proteins in small amounts of blood serum and plasma. Amer. J. clin. Path., techn. sect. 10, 40–49 (1946)Google Scholar

Copyright information

© Springer-Verlag 1974

Authors and Affiliations

  • E. D. Wachsmuth
    • 1
    • 2
  • A. Torhorst
    • 1
    • 2
  1. 1.Friedrich Miescher-InstitutBaselSwitzerland
  2. 2.Biochemisch-Immunologische Abteilung des Pathologischen Instituts der Technischen Universität MünchenMünchenFederal Republic of Germany

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