Skip to main content
Log in

Improved histochemical method for the demonstration of the activity of α-glucan phosphorylase

I. The use of glucosyl acceptor dextran

  • Published:
Histochemie Aims and scope Submit manuscript

Summary

A modified method for the histochemical demonstration of the activity of α-glucan phosphorylase is described. In the histochemical system the enzyme catalyses the synthesis of glycogen by transglucosylation from α-d-glucosylphosphate. The incubation medium contains dextran as glucosyl acceptor. Therefore, in contrast with the unmodified method, the new technique is able to demonstrate the activity of phosphorylase in ischaemic glycogen-depleted tissues.

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

  • Bajusz, E., and G. Jasmin: Histochemical studies on the myocardium following experimental interference with coronary circulation in the rat. Acta histochem. (Jena) 18, 222–237 (1964).

    Google Scholar 

  • Cori, G. T., B. Illingworth, and P.J. Keller: Muscle phosphorylase: In: Methods in enzymology, ed. by S. P. Colowick and N. O. Kaplan, vol.1, p. 200–206. New York: Academic Press 1955.

    Google Scholar 

  • Cornblath, M., P. J. Randle, A. Parmeggiani, and H. E. Morgen: Regulation of glycogenolysis in muscle. J. biol. Chem. 238, 1592–1957 (1963).

    Google Scholar 

  • Durrer, D., R. T. van Dam, G. Freud, F. L. Meyler, J. Snijder, A. E. F. H. Meijer, and C. A. Wagenvoort: To be published.

  • Eränkö, O., and A. Palkama: Improved localization of phosphorylase by the use of polyvinylpyrrolidone and high substrate concentration. J. Histochem. Cytochem. 9, 585 1961).

    Google Scholar 

  • Fine, G., A. Morales, and J. R. Scerpella: Experimental myocardial infarction. Arch. Path. 82, 4–15 (1966).

    Google Scholar 

  • Godlewsky, H. G.: Are active and inactive phosphorylases histochemically distinguishable ? J. Histochem. Cytochem. 11, 108–112 (1963).

    Google Scholar 

  • Hecht, A.: Das Verhalten der histochemisch nachweisbaren Phosphorylaseaktivität am anoxischruhenden und anoxischtätigen Rattenherzmuskel. Histochemie 9, 48–57 (1967).

    Google Scholar 

  • Heene, R.: Hemmung Glycogenbildender Enzyme durch 2,4-Dichlorphenoxyazetat. Histochemie 8, 45–53 (1967).

    Google Scholar 

  • Henion, W. F., and E. W. Sutherland: Immunological differences of phosphorylases. J. biol. Chem. 224, 477–488 (1957).

    Google Scholar 

  • Krebs, E. G., and E. H. Fischer: Phosphorylase activity of skeletal muscle extracts. J. biol. Chem. 216, 113–120 (1955).

    Google Scholar 

  • Parmeggiani, A., and H. E. Morgan: Effect of adenine nucleotides and inorganic phosphate on muscle phosphorylase activity. Biochem. Biophys. Res. Commun. 9, 252–256 (1962).

    Google Scholar 

  • Seiferth, J.: Fermenthistochemische Frühveränderungen des experimentellen Myokardinfarktes bei der Ratte. Frankfurt. Z. Path. 76, 329–339 (1967).

    Google Scholar 

  • Sutherland, E. W.: The effect of the hyperglycemic factor and epinephrine on enzyme systems of liver and muscle. Ann. N. Y. Acad. Sci. 54, 693–706 (1951).

    Google Scholar 

  • Takeuchi, T. K., K. Higashi, and S. Watanuki: Distribution of amylophosphorylase in various tissues of human and mammalian organs. J. Histochem. Cytochem. 3, 485–491 (1955).

    Google Scholar 

  • Wu, R., and E. Racker: Described by: R. Schmid, P. W. Robbins and R. R. Traut: Glycogen synthesis in muscle lacking phosphorylase. Proc. Nat. Acad. Sci. (Wash.) 45, 1236–1240 (1959).

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Meijer, A.E.F.H. Improved histochemical method for the demonstration of the activity of α-glucan phosphorylase. Histochemie 12, 244–252 (1968). https://doi.org/10.1007/BF00306002

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00306002

Keywords

Navigation