Skip to main content
Log in

Rat liver 5′-nucleotidase

  • Papers
  • Published:
The Histochemical Journal Aims and scope Submit manuscript

Synopsis

Under assay conditions such that there is minimal interference by lysosomal acid phosphatase, the dephosphorylation of nucleoside-5′-monophosphates (AMP or UMP) by rat-liver homogenates at alkaline pH values is attributable to a Mg2+-dependent enzyme (5′-nucleotidase, EC 3.1.3.5). It shows a bimodal distribution between the nuclear and the microsomal fractions, different from that for glucose-6-phosphatase, and also differs in its response to deoxycholate. There is no evidence of an endogenous inhibitor or of enzyme latency. No clear evidence for the existence of more than one 5′-nucleotidase has come from the approaches adopted. These include differential centrifugation, trial of different ions as activators and inhibitors, determination of pH curves, mixed-substrate assays, column chromatography, and the study of liver regeneration (which depresses the activity) and of hepatocarcinogenesis. Results obtained with maleate, Pb2+ ions and Ni2+ ions have a bearing on histochemical and clinical work. The ‘acid phosphatase’ activity of lysosome-rich fractions towards β-glycerophosphate, 5′-AMP, 5′-UMP and 2′-(3′-)UMP, at pH values near 5.0 with no divalent cations added, seems to be due to a single enzyme or group of isoenzymes. The effects of certain anions and cations on this lysosomal activity, and on microsomal 5′-nucleotidase activity, depend on the concentration of the substrate as well as on its nature.

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

  • Arsenis, C. &Touster, O. (1967). The partial resolution of acid phosphatase of rat liver lysosomes into a nucleotidase and a sugar phosphate phosphohydrolase.J. biol Chem. 242, 3399–401.

    Google Scholar 

  • Barka, T. (1961). Studies on acid phosphatases. II. Chromatographic separation of acid phosphatases of rat liver.J. Histochem. Cytochem. 9, 564–71.

    PubMed  Google Scholar 

  • Bodansky, O. &Schwartz, M. K. (1963). Comparative effects ofl-histidine on the activities of 5′-nucleotidase and alkaline phosphatase.J. biol. Chem. 238, 3420–7.

    PubMed  Google Scholar 

  • Campbell, D. M. (1962). Determination of 5-nucleotidase in blood serum.Biochem. J. 82, 34P.

    Google Scholar 

  • Cochran, K. W., Zerwic, M. M. &Dubois, K. P. (1951). Studies of the mechanism of acute beryllium poisoning.J. Pharmac. exp. Ther. 102, 165–78.

    Google Scholar 

  • De Duve, C., Pressman, B. C., Gianetto, R., Wattiaux, R. &Appelmans, F. (1955). Tissue fractionation studies: 6. Intracellular distribution patterns of enzymes in rat-liver tissue.Biochem. J. 60, 604–17.

    PubMed  Google Scholar 

  • De Lamirande, G., Allard, C. &Cantero, A. (1958). Intracellular distribution of 5′-nucleotidase in rat liver.J. biophys. biochem. Cytol. 4, 373–6.

    PubMed  Google Scholar 

  • El-Aaser, A. A., Fitzsimons, J. T. R., Hinton, R. H., Reid, E., Klucics, E. &Alexander, P. (1966b). Zonal centrifugation of crude nuclear fractions from liver.Biochim. biophys. Acta 127, 553–6.

    PubMed  Google Scholar 

  • El-Aaser, A. A. & Reid, E. (1965). Rat liver 5′-nucleotidase. Abstracts of communications, 2nd mtg. Fed. Europ. Biochem. Societies, 41.

  • El-Aaser, A. A. &Reid, E. (1969). Phosphatase activities in rat liver before and after birth.Histochem. J. 1, 439–58.

    PubMed  Google Scholar 

  • El-Aaser, A. A., Reid, E., Klucics, E., Alexander, P., Lett, J. T. &Smith, J. (1966a). Resolution of the components in the microsomal fraction of liver in the B-IV zonal centrifuge.Nat. Cancer Inst. Monogr. 21, 323–32.

    PubMed  Google Scholar 

  • Emmelot, P., Bos, C. J., Benedetti, E. L. &Rümke, P. H. (1964). Studies on plasma membranes. I. Chemical composition and enzyme content of plasma membranes isolated from rat liver.Biochim. biophys. Acta 90, 126–45.

    PubMed  Google Scholar 

  • Ernster, L. &Jones, L. C. (1962). Enzyme structure relationships in the endoplasmic reticulum of rat liver.J. Cell. Biol. 15, 541–62.

    Google Scholar 

  • Fritzson, P. (1967). Dephosphorylation of pyrimidine nucleotides in the soluble fraction of homogenates from normal and regenerating rat liver.European J. Biochem. 1, 12–20.

    Google Scholar 

  • Goldfischer, S., Essner, E. &Novikoff, A. B. (1964). The localization of phosphatase activities at the level of ultrastructure.J. Histochem. Cytochem. 12, 72–95.

    PubMed  Google Scholar 

  • Goodlad, G. A. J. &Mills, G. T. (1957). The acid phosphatases of rat liver.Biochem. J. 66, 346–54.

    PubMed  Google Scholar 

  • Hardonk, M. J. &De Boer, H. G. A. (1968). 5′-nucleotidase. III. Determinations of 5′-nucleotidase isoenzymes in tissue of rat and mouse.Histochemie 12, 29–41.

    PubMed  Google Scholar 

  • Hill, P. G. &Sammons, H. G. (1966). An automated method for the determination of serum 5′-nucleotidase.Clin. Chim. Acta 13, 739–45.

    PubMed  Google Scholar 

  • Hinton, R. H., Klucics, E., El-Aaser, A. A., Fitzsimons, J. T. R., Alexander, P. & Reid, E. (1967). Zonal centrifugation of hepatic microsomal material.Biochem. J. 105, 14P.

  • Itoh, R., Mitsui, A. &Tsushima, K. (1967). 5′-nucleotidase of chicken liver.Biochim. biophys. Acta 146, 151–9.

    PubMed  Google Scholar 

  • Kaye, M. A. G. (1955). The effect of zinc on 5-nucleotidase of cobra venom and the interference of other nucleotides.Biochim. biophys. Acta 18, 456–8.

    PubMed  Google Scholar 

  • Ku, K-Y. &Wang, C-T (1963). 5′-nucleotidase of isolated hepatic cell membrane from rat liver.Acta Biol. Exp. Sinica 8, 400–7. Cited inChem. Abstr. 61, 2123 (1964).

    Google Scholar 

  • Landau, W. &Schlamowitz, M. (1961). Studies of factors related to the differentiation of alkaline phosphates derived from several tissues.Archs. Biochem. Biophys. 95, 474–82.

    Google Scholar 

  • Lowry, O. H. &Lopez, J. A. (1946). The determination of inorganic phosphate in the presence of labile phosphate esters.J. biol. Chem. 162, 421–8.

    Google Scholar 

  • Moore, B. W. &Angeletti, P. V. (1961). Chromatographic heterogeneity of some enzymes in normal tissues and tumours.Ann. N.Y. Acad. Sci. 94, 659–67.

    PubMed  Google Scholar 

  • Neil, M. W. &Horner, M. W. (1964). Studies on acid hydrolases in adult and foetal tissues. Acidp-nitrophenyl phosphate phosphohydrolases of adult guinea-pig liver.Biochem. J. 92, 217–24.

    PubMed  Google Scholar 

  • Novikoff, A. B. (1963). Lysosomes in the physiology and pathology of cells: Contributions of staining methods. InLysosomes, pp. 36–73. (ed. A. V. S. de Reuck & M. P. Cameron). London: Churchill.

    Google Scholar 

  • Novikoff, A. B. (1964). Membrane-bound enzymes.Abstracts, 6th Internat. Congr. Biochem. 609–10.

  • Reid, E. (1964). Azo-dye carcinogenesis: enzymes concerned in uridine nucleotide metabolism.Brit. J. Cancer 18, 179–96.

    PubMed  Google Scholar 

  • Reid, E. (1967).Enzyme Cytology, p. 321 (ed. D. B. Roodyn). London: Academic Press.

    Google Scholar 

  • Reid, E., El-Aaser, A. A., Turner, M. K. &Siebert, G. (1964). Enzymes of ribonucleic acid and ribonucleotide metabolism in rat liver nuclei.Hoppe-Seyler's Z. für physiol. Chem. 339, 135–49.

    Google Scholar 

  • Reid, E. &Stevens, B. M. (1958). Hormones and liver cytoplasm. 5. Enzymes concerned in nucleic acid catabolism, as affected by hypophysectomy or adrenalectomy.Biochem. J. 68, 367–74.

    PubMed  Google Scholar 

  • Segal, H. L. &Brenner, R. M. (1960). 5′-nucleotidase of rat liver microsomes.J. biol. Chem. 235, 471–4.

    PubMed  Google Scholar 

  • Shibko, S. &Tappel, A. L. (1963). Acid phosphatase of the lysosomal and soluble fraction of rat liver.Biochim. biophys. Acta 73, 76–86.

    PubMed  Google Scholar 

  • Siekevitz, P. (1965). Origin and functional nature of microsomes.Fedn. Proc. 24, 1153–5.

    Google Scholar 

  • Song, C. S. &Bodansky, O. (1967). Subcellular localization and properties of 5′-nucleotidase in the rat liver.J. biol. Chem. 242, 694–9.

    PubMed  Google Scholar 

  • Sonnenscheim, M. &Kopac, M. J. (1955). The phosphatase activities of the microsomal (submicroscopic particulate) fraction prepared in an electrolyte medium.J. cell. comp. Physiol. 45, 361–75.

    Google Scholar 

  • Wachstein, M. &Meisel, E. (1957). Histochemistry of hepatic phosphatases at a physiologic pH with special reference to the demonstration of bile canaliculi.Am. J. clin. Path. 27, 13–23.

    PubMed  Google Scholar 

  • Wang, D. Y. (1962). Variation of 5′-nucleotidase activity of the rat mammary gland during pregnancy, lactation and involution.Biochem. J. 83, 633–7.

    Google Scholar 

  • Weser, U. (1968). Reaction of some transition metals with nucleic acids and their constituents. InStructure and Bonding, Vol. 5, pp. 41–67. Berlin: Springer-Verlag.

    Google Scholar 

  • Whitcutt, J. M., Sutton, D. A. &Nunn, J. R. (1960). Carcinogenesis: changes in the properties of some rat-liver proteins after administration of 4-dimethylamino-3′-methylazobenzene.Biochem. J. 75, 557–62.

    PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Additional information

A. A. El-Aaser is on leave from the Faculty of Medicine, University of Cairo

Rights and permissions

Reprints and permissions

About this article

Cite this article

El-Aaser, A.A., Reid, E. Rat liver 5′-nucleotidase. Histochem J 1, 417–437 (1969). https://doi.org/10.1007/BF01086983

Download citation

  • Received:

  • Revised:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01086983

Keywords

Navigation