Skip to main content
Log in

Electrophoretic and histochemical studies of carbonic anhydrase activity

  • Published:
Histochemie Aims and scope Submit manuscript

Summary

A simple method for separation of carbonic anhydrase activity into components by electrophoresis on cellulose acetate strips is described. With this method, using barbiturate buffer systems at various pH values, two main components of CAH in rat erythrocytes, and the splitting of each of these into two minor components were revealed. Two components were also observed in the CAH activity in kidney and lens homogenates, and one component in brain homogenate. A modification of Häusler's histochemical method for CAH was adapted for visualization of the electrophoretically separated bands. This rendered the evalution of the results easier than with the quantitative measurements alone. The quantitative measurement of CAH activity in electrophoretic strips corresponded with the degree of staining by the histochemical method. This among other facts supports the view of the specificity of the histochemical method used. Some examples of the histochemical staining pattern of the CAH activity in rat tissues are given.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Aronson, T., and A. Grönwall: Improved separation of serum proteins in paper electro phoresis — a new electrophoresis buffer. Scand. J. clin. Lab. Invest. 9, 338–341 (1957).

    Google Scholar 

  • Berliner, R. W., and J. Orloff: Carbonic Anhydrase Inhibitors. Pharmacol. Rev. 8, 137–174 (1956).

    Google Scholar 

  • Bleyl, U.: Zur Spezifität des Histochemischen Carbonanhydratasenachweis im Inselorgan der Bauchspeicheldrüse. Histochemie 4, 286–311 (1964).

    Google Scholar 

  • Edsall, J. T.: Recent advances in protein research. In: New perspectives in biology, ed. by M. Sela, vol. 4, p. 6–12. Amsterdam: Elsevier Publ. Co. 1964.

    Google Scholar 

  • Fand, S. B., H. J. Levine, and H. L. A. Ervin: A reapraisal of the histochemical method for carbonic anhydrase. J. Histochem. Cytochem. 7, 27–30 (1959).

    Google Scholar 

  • Giacobini, E.: Localization of carbonic anhydrase in the nervous system. Science 134, 1524–1525 (1961).

    Google Scholar 

  • Häusler, G.: Zur Technik und Spezifität des histochemischen Carboanhydrasenachweises im Modellversuch und in Gewebeschnitten von Rattennieren. Histochemie 1, 29–47 (1958).

    Google Scholar 

  • Henriques, O. M.: Carbonahydrase. Ergebn. Physiol. 28, 1–20 (1929).

    Google Scholar 

  • Korhonen, E., and L. K. Korhonen: Histochemical demonstration of carbonic anhydrase activity in the eyes of rat and mouse. Acta ophthal. (Kbh.) (in the press).

  • Korhonen, L. K., E. Näätänen, and M. Hyyppä: A histochemical study of carbonic anhydrase in some parts of the mouse brain. Acta histochem. (Jena) 18, 336–347 (1964).

    Google Scholar 

  • Kurata, Y.: Histochemical demonstration of carbonic anhydrase activity. Stain Technol. 28, 231–233 (1953).

    Google Scholar 

  • Laurent, G., C. Marriq, D. Nahon, M. Charrel et Y. Derrien: Isoelement des protéines 2«lentes2» Y, X1, et X2 accompagnant l'hémoglobine humaine dans ses préparations. C. R. Soc. Biol. (Paris) 156, 1456–1461 (1962).

    Google Scholar 

  • Lindskog, S.: Purification and properties of bovine erythrocyte carbonic anhydrase. Biochim. biophys. Acta (Amst.) 39, 218–226 (1960).

    Google Scholar 

  • Meldrum, N. U., and F. J. W. Roughton: Carbonic anhydrase. Its preparation and properties. J. Physiol. (Lond.) 80, 113–143 (1933).

    Google Scholar 

  • Nyman, P. O.: Purification and properties of carbonic anhydrase from human erythrocytes. Biochim. biophys. Acta (Amst.) 52, 1–12 (1961).

    Google Scholar 

  • Pearse, A. G. E.: Histochemistry, theoretical and applied. London: Churchill Ltd. 1960.

    Google Scholar 

  • Poulik, M. D.: Starch gel electrophoresis in a discontinuous system of buffers. Nature (Lond.) 180, 1477–1479 (1957).

    Google Scholar 

  • Rickli, E., A. S. Ghazanfar, B. H. Gibbons, and J. T. Edsall: Carbonic anhydrase from human erythrocytes. J. biol. Chem. 239, 1065–1079 (1964).

    Google Scholar 

  • Roughton, F. J. W., and V. H. Booth: The effect of substrate concentration, pH and other factors upon the activity of carbonic anhydrase Biochem. J. 40, 309–330 (1946).

    Google Scholar 

  • Scott, D. A., and J. Fisher: Carbonic anhydrase. J. biol. Chem. 144, 371–381 (1942).

    Google Scholar 

  • Sen, M., S. M. Drance, and V. R. Woodford: Separation of bovine lens carbonic anhydrase into two components. Canad. J. Biochem. 41, 1235–1241 (1963).

    Google Scholar 

  • Smith, E. L.: Mode of action of the metal peptidases. Proc. nat. Acad. Sci. (Wash.) 35, 80–90 (1949).

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Korhonen, L.K., Korhonen, E. Electrophoretic and histochemical studies of carbonic anhydrase activity. Histochemie 5, 279–288 (1965). https://doi.org/10.1007/BF00285793

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00285793

Keywords

Navigation