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Über den Einfluß der Gelinkubation mit Polyvinylalkohol auf die Löslichkeit der Fructose-1,6-diphosphat-Aldolase

The effect of gel incubation using polyvinyl alcohol on the solubility of fructose-1,6-diphosphate-aldolase

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Summary

The decrease in the solubility of fructose- 1,6-diphosphate-aldolase (fructose-1, 6-diphosphate-D-glyceraldehyde-3-phosphate lyase, E.C.4.1.2.13) brought about by the addition of polyvinyl alcohol to the incubation medium was tested observing histochemical conditions. After 100 minutes of incubation in an aqueous medium less than 10% of the original enzymic activity was demostrated in sections of rat cardiac muscle and kidney. After polyvinyl alcohol was added to the incubation medium the enzymic activity in the sections (measured over the same period) was 80% in rat cardiac muscle and 30–40% in kidney sections. The importance of these findings for the histochemical demonstration of aldolase is shown in the rat cardiac muscle. The organ dependend differences in the solubility may find an explanation in the presence of various iso-enzymes in the two organs under investigation.

Zusammenfassung

Die Verminderung der Löslichkeit der Fructose-1,6-diphosphat-Aldolase (Fructose-1,6-diphosphat-D-Glycerinaldehyd-3-phosphat-Lyase, E.C. 4.1.2.13) durch Zusatz von Polyvinylalkohol zum Inkubationsmedium wurde unter Einhaltung histochemischer Bedingungen überprüft. Bei der Inkubation in wäßrigem Medium sind nach 100 min in einem Schnitt des Herzmuskels und der Niere der Ratte weniger als 10% der ursprünglichen Enzymaktivität nachweisbar. Nach Zusatz von Polyvinylalkohol zum Inkubationsmedium beträgt die im Schnitt verbleibende Enzymaktivität nach gleicher Inkubationsdauer für den Rattenherzmuskel etwa 80%, für die Niere 30–40%. Die Bedeutung dieser Befunde für den histochemischen Nachweis der Aldolase wird am Beispiel des Rattenherzmuskels gezeigt. Als Ursache der organbedingten Unterschiede im Löslichkeitsverhalten wird die Anwesenheit verschiedener Isoenzyme in beiden Organen in Betracht gezogen.

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Literatur

  • Altman, F. P., and J. Chayen: Retention of nitrogenous material in unfixed sections during incubation for histochemical demonstration of enzymes. Nature (Lond.) 207, 1205 (1965).

    Article  Google Scholar 

  • Arnold, F., K. D. Kunze u. H. Simon: Zur Problematik des histotopochemischen Nachweises der Fructose-1,6-diphosphat-Aldolase am Beispiel der Rattenniere. Histochemie 9, 84–92 (1967).

    Article  CAS  PubMed  Google Scholar 

  • Benitez, L., and R. Fischer: A modification to the “Incubation mixture Film method” for the histochemical localization of lactic dehydrogenase. J. Histochem. Cytochem. 12, 858–859 (1964).

    Article  CAS  PubMed  Google Scholar 

  • Christen, Ph., U. Rensing, A. Schmid u. F. Leuthardt: Multiple Formen der Aldolase in Organextrakten der Ratte. Helv. chim. Acta 49, 1872–1875 (1966).

    Article  CAS  PubMed  Google Scholar 

  • Fahimi, H. D. and C. R. Amarasingham: Cytochemical localization of lactic dehydrogenase in white skeletal muscle. J. Cell Biol. 22, 29–48 (1964).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Farber, E.: Control studies on the histochemical localization of spezific DPN-linked dehydrogenases. J. Histochem. Cytochem. 10, 657–658 (1962).

    Google Scholar 

  • Fine, I. H., and L. A. Costello: The use of starch electrophoresis in dehydrogenase studies. Methods in Enzymology 6, 958–972 (1963).

    Article  CAS  Google Scholar 

  • Freimuth, U., H. Grossmann u. B. Johannsen: Zur Methode der Elektrophorese in Stärkegel. Arbeitsvorschrift u. Beispiele im Hinblick auf ihre Anwendung in der analytischen Praxis. Z. med. Labortechn. 6, 333–339 (1965).

    Google Scholar 

  • Friede, R. L., L. M. Fleming, and M. Knoller: A quantitative appraisal of enzyme histochemical methods in brain tissue. J. Histochem. Cytochem. 11, 232–245 (1963).

    Article  CAS  Google Scholar 

  • Herskovits, J. J., C. J. Masters, P. M. Wassarman, and N. O. Kaplan: On the tissue specifity and biological significance of aldolase C in the chicken. Biochem. biophys. Res. Commun. 26, 24–29 (1967).

    Article  CAS  PubMed  Google Scholar 

  • Janata, V., J. Fischer, L. Jilek, and V. Malik: The diffusion of lactate, succinate and glutamate dehydrogenase from cryostat tissue of the brain of rats into the incubating medium during ontogeny. Acta histochem. (Jena) 26, 28–35 (1967).

    CAS  Google Scholar 

  • Jones, G. R. N., A. J. Maple, E. K. Aves, J. Chayen, and G. J. Cunningham: Quantitative histochemistry of succinate dehydrogenase in tissue sections. Nature (Lond.) 197, 568–570 (1963).

    Article  CAS  Google Scholar 

  • Kalina, M., and P. B. Gahan: A quantitative study of the validity of the histochemical demonstration for pyridine-nucleotide-linked dehydrogenases. Histochemie 5, 430–436 (1965a).

    Article  CAS  PubMed  Google Scholar 

  • —: An evaluation of the demonstration of certain pyridine-nucleotide-linked dehydrogenases. Nature (Lond.) 207, 647–648 (1965b).

    Article  CAS  Google Scholar 

  • Lojda, Z.: Remarks on histochemical demonstration of dehydrogenases. II. Intracellular localization. Folia morph. (Warszawa) 13, 84–96 (1965).

    CAS  Google Scholar 

  • Mathisen, J. S., and S. I. Mellgren: Some observations concerning the role of phenazine methosulfate in histochemical dehydrogenase methods. J. Histochem. Cytochem. 13, 408–409 (1965).

    Article  CAS  PubMed  Google Scholar 

  • McMillan, P. J.: Differential demonstration of muscle and heart type lactic dehydrogenase of rat muscle and kidney. J. Histochem. Cytochem. 15, 21–31 (1967).

    Article  CAS  Google Scholar 

  • Pette, D., and H. Brandau: Intracellular localization of glycolytic enzymes in cross-striated muscles of Locusta migratoria. Biochem. biophys. Res. Commun. 9, 367–370 (1962).

    Article  CAS  PubMed  Google Scholar 

  • —: Enzym-Histiogramme und Enzymaktivitätsmuster der Rattenleber, Nachweis Pyridinnukleotidspezifischer Dehydrogenasen im Gelschicht-Verfahren. Enzym. biol. clin. 6, 79–122 (1966).

    CAS  Google Scholar 

  • Pietruszko, R., and D. N. Baron: A staining procedure for demonstration of multiple forms of aldolase. Biochim. biophys. Acta (Amst.) 132, 203–206 (1967).

    Article  CAS  Google Scholar 

  • Rensing, U., A. Schmid u. F. Leuthardt: Veränderungen im Isoenzymmuster der Aldolase aus Rattenorganen während der Entwicklung. Hoppe-Seyler's Z. physiol. Chem. 348, 921–928 (1967).

    Article  CAS  PubMed  Google Scholar 

  • Sibley, J. A., and A. L. Lehninger: Determination of aldolase in animal tissues. J. biol. Chem. 177, 859–872 (1949).

    CAS  PubMed  Google Scholar 

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Arnold, F., Kunze, K.D. & Grossmann, H. Über den Einfluß der Gelinkubation mit Polyvinylalkohol auf die Löslichkeit der Fructose-1,6-diphosphat-Aldolase. Histochemie 13, 196–202 (1968). https://doi.org/10.1007/BF00266581

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  • DOI: https://doi.org/10.1007/BF00266581

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