Skip to main content
SpringerLink
Log in

Degradation of Purine Nucleotides

  • Chapter
Uric Acid

Part of the book series: Handbook of Experimental Pharmacology ((HEP,volume 51))

Abstract

Purine nucleotides have a vital role in metabolism. Therefore, the maintenance of a constant nucleotide composition of the cell is essential for normal function. Purine nucleotides are synthesized by purine biosynthesis de novo, by salvage pathways and nucleoside kinases, and by degradation of nucleic acids. The use of nucleotides occurs in nucleic acid synthesis, in various reactions of intermediary metabolism and in the degradation to the inert product uric acid. Regulated activity of these many pathways by synthesizing and degrading nucleotides appears to be critical.

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

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 84.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Agarwal, K.C., Agarwal, R.P., Stockier, J.D., Parks, Jr., R.E.: Purine nucleside Phosphorylase. Microheterogeneity and comparison of kinetic behavior of the enzyme from several tissues and species. Biochemistry 14, 79–84 (1975)

    PubMed  CAS  Google Scholar 

  • Agarwal, R.P., Crabtree, G.W., Parks Jr., R.E., Nelson, J.A., Keightly, R., Parkman, R., Rosen, F.S., Stern, R.C., Polmar, S.H.: Purine nucleoside metabolism in the erythrocytes of patients with adenosine deaminase deficiency and severe combined immunodeficiency. J. clin. Invest. 57, 1025–1035 (1976)

    PubMed  CAS  Google Scholar 

  • Agarwal, R.P., Parks Jr., R.E.: Purine nucleoside Phosphorylase from human erythrocytes: crystallization and some properties. J. biol. Chem. 244, 644–647 (1969)

    PubMed  CAS  Google Scholar 

  • Akedo, H., Nishihara, H., Shinkai, K., Komatsu, K., Ishikawa, S.: Multiple forms of human adenosine deaminase I purification and characterization of two molecular species. Biochim. biophys. Acta (Amst.) 276, 257–271 (1972)

    CAS  Google Scholar 

  • Ali, S., Sitaramayya, A., Kumar, K.S., Krishnam, P.S.: Guanine deaminase inhibitor from rat livers: isolation and characterization. Biochem. J. 137, 85–92 (1974)

    PubMed  CAS  Google Scholar 

  • Bachorik, P.S., Dietrich, L.S.: The purification and properties of detergent-solubilized rat liver nucleotide pyrophosphatase. J. biol. Chem. 247, 5071–5078 (1972)

    PubMed  CAS  Google Scholar 

  • Benke, P.J., Dittmar, D.: Purine dysfunction in cells from patients with adenosine deaminase deficiency. Pediat. Res. 10, 642–646 (1976)

    PubMed  CAS  Google Scholar 

  • Bergeron, J. J.M., Berridge, M.V., Evans, W.H.V.: Biogenesis of plasmalemmal glycoproteins. Intracellular site of synthesis of mouse liver plasmalemmal 5′-nucleotidase as determined by the subcellular location of messenger RNA coding for 5′-nucleotidase. Biochim. biophys. Acta (Amst.) 407, 325–337 (1975)

    CAS  Google Scholar 

  • Berne, R.M., Rubio, R., Dobson, J.O., Curnish, R.R.: Adenosine and adenine nucleotides as possible mediators of cardiac and skeletal muscle blood flow regulation. Circulat. Res. 28/29(Suppl.1), 115–119(1971)

    Google Scholar 

  • Bischoff, E., Tran-Thi, T., Decker, K.F.A.: Nucleotide pyrophosphatase of rat liver: a comparative study on the enzymes solubilized and purified from plasma membrane and endoplasmic reticulum. Europ. J. Biochem. 51, 353–361 (1975)

    PubMed  CAS  Google Scholar 

  • Bischoff, I., Wilkening, J., Tran-Thi, T., Decker, K.: Differentiation of the nucleotide pyrophosphatases of rat liver plasma membrane and endoplasmic reticulum by enzymic iodination. Europ. J. Biochem. 62, 279–283 (1976)

    PubMed  CAS  Google Scholar 

  • Bode, J.C., Zelder, O., Rumpelt, H.J., Wittkamp, U.: Depletion of liver adenosine phosphates and metabolic effects of intravenous infusion of fructose or sorbital in man and in the rat. Europ. J. clin. Invest. 3, 436–441 (1973)

    PubMed  CAS  Google Scholar 

  • Bosmann, H.B., Pike, G.: Membrane marker enzymes: isolation, purification and properties of 5′-nucleotidase from rat cerebellum. Biochim. biophys. Acta (Amst.) 227, 402–417 (1971)

    CAS  Google Scholar 

  • Bourne, H.R., Lichtenstein, L.M., Melmon, K.L., Henney, C.S., Weinstein, Y., Shearer, G.M.: Modulation of inflammation and immunity by cyclic AMP. Science 184, 19–28 (1974)

    PubMed  CAS  Google Scholar 

  • Brady, T.G., O’Connell, N.: A purification of adenosine deaminase from the superficial mucosa of calf intestine. Biochim. biophys. Acta (Amst.) 62, 216–229 (1962)

    CAS  Google Scholar 

  • Bray, R.C.: Xanthine oxidase. In: Boyer, P., Lardy, H., Myrbach, K. (Eds.): The Enzymes, 2nd Ed., p. 533. New York: Academic Press 1963

    Google Scholar 

  • Brownlee, S.T., Heath, E.C.: An extracellular 5′-nucleotidase with both monoesterase and diesterase activity from micrococcus sodonensis. Arch. Biochem. Biophys. 166, 1–7 (1975)

    PubMed  CAS  Google Scholar 

  • Burch, H.B., Lowry, O.H., Meinhardt, L., Max Jr., P., Chyu, K.: Effect of fructose, dihydroxyace-tone, glycerol and glucose on metabolites and related compounds in liver and kidney. J. biol. Chem. 245, 2092–2102 (1970)

    PubMed  CAS  Google Scholar 

  • Burger, R.M., Lowenstein, J.M.: 5′-nucleotidase from smooth muscle of small intestine and from brain. Inhibition of nucleotides. Biochemistry 14, 2362–2366 (1975)

    PubMed  CAS  Google Scholar 

  • Burnstock, G.: Purinergic nerves. Pharmacol. Rev. 24, 509–581 (1972)

    PubMed  CAS  Google Scholar 

  • Bynum, J.W., Volkin, E.: Wasting of 18 S ribosomal RNA by human myeloma cells cultured in adenosine. J. Cell Physiol. 88, 197–206 (1976)

    PubMed  CAS  Google Scholar 

  • Carson, D.A., Goldblum, R., Keightley, R., Seegmiller, J.E.: Immunochemical analysis of adenosine deaminase in combined immunodeficiency disease. J. Clin. Chem. Clin. Biochem. 14, 283 (1976)

    Google Scholar 

  • Carson, D.A., Seegmiller, J.E.: Effect of adenosine deaminase inhibition upon human lymphocyte blastogenesis. J. clin. Invest. 57, 274–282 (1976)

    PubMed  CAS  Google Scholar 

  • Catignani, G.L., Chytil, F., Darby, W.J.: Vitamin E deficiency: immunochemical evidence for increased accumulation of liver xanthine oxidase. Proc. nat. Acad. Sci. (Wash.) 71, 1966 – 1968 (1974)

    CAS  Google Scholar 

  • Center, M.S., Behal, F.J.: Calf intestinal 5′-nucleotidase. Arch. Biochem. Biophys. 114, 414–421 (1966)

    CAS  Google Scholar 

  • Cercignani, G., Serra, M.C., Fini, C., Natalini, P., Palmerini, C.A., Magni, G., Ipata, P.L.: Properties of 5′-nucleotidase from Bacillus cereus obtained by washing intact cells with water. Biochemistry 13, 3628–3634 (1974)

    PubMed  CAS  Google Scholar 

  • Chen, S., Scott, R.C., Swedberg, R.K.: Heterogeneity for adenosine deaminase deficiency; expression of the enzyme in cultured skin fibroblasts and amniotic fluid cells. Amer. J. hum. Genet. 27, 46–52(1975)

    PubMed  CAS  Google Scholar 

  • Clark, R.B., Seney, M.N.: Regulation of adenylate cyclase from cultured human cell lines by adenosine. J. biol. Chem. 251, 4239–4246 (1976)

    PubMed  CAS  Google Scholar 

  • Coddington, A.: Some substrates and inhibitors of adenosine deaminase. Biochim. biophys. Acta (Amst.) 99, 442–451 (1965)

    CAS  Google Scholar 

  • Cohen, A., Doyle, D., Martin, Jr., D.W., Ammann, A. J.: Abnormal purine metabolism and purine overproduction in a patient deficient in purine nucleoside Phosphorylase. New Engl. J. Med. 295, 1449–1454 (1976)

    PubMed  CAS  Google Scholar 

  • Cory, J.G., Weinbaum, G., Suhadolnik, R. J.: Multiple forms of calf serum adenosine deaminase. Arch. Biochem. Biophys. 118, 428–433 (1967)

    CAS  Google Scholar 

  • Coulson, R.: Metabolism and excretion of exogenous adenosine 3′: 5′-monophosphate and guanosine 3′: 5′-monophosphate: studies in the isolated perfused kidney and in the intact rat. J. biol. Chem. 251, 4958–4967 (1976)

    PubMed  CAS  Google Scholar 

  • Crabtree, G.W.C., Henderson, J.F.: Pathways of purine ribonucleotide catabolism in Ehrlich ascites tumor cells in vitro. Canad. J. Biochem. 49, 959–963 (1971)

    CAS  Google Scholar 

  • Creagan, R.P., Tischfield, J. A., Nichols, E. A., Ruddle, F.H.: Autosomal assignment of the gene for the form of adenosine deaminase which is deficient in patients with combined immunodeficiency syndrom. Lancet 1973II, 1449

    Google Scholar 

  • Currie, R., Bergel, F., Bray, R.C.: Enzymes and cancer: preparation and some properties of guanase from rabbit liver. Biochem. J. 104, 634–638 (1967)

    PubMed  CAS  Google Scholar 

  • Daddona, P., Kelley, W.N.: Human adenosine deaminase purification and subunit structure. J. biol. Chem. 252, 110–115 (1977)

    PubMed  CAS  Google Scholar 

  • Daddona, P., Van der Weyden, M.B., Kelley, W.N.: Characterization of human adenosine deaminase. Clin. Res. 24, 575 A (1976)

    Google Scholar 

  • De Boeck, S., Rymen, T., Stockx, J.: Adenosine deaminase in chicken-egg yolk and its relation to homologous enzymes in liver and plasma of the adult hen. Europ. J. Biochem. 52, 191–195 (1975)

    PubMed  Google Scholar 

  • Debray, H., Cartier, P., Temstet, A., Cendron, J.: Child’s urinary lithiasis revealing a complete deficit in adenine phosphoribosyltransferase. Pediat. Res. 10, 762–766 (1976)

    PubMed  CAS  Google Scholar 

  • Divekar, A.Y.: Adenosine Phosphorylase activity as distinct from inosine-guanosine Phosphorylase activity in sarcoma 180 cells and rat liver. Biochim. biophys. Acta (Amst.) 422, 15–28 (1976)

    CAS  Google Scholar 

  • Drummond, G.I., Yamamoto, M.: Nucleotide phosphomonoesterases: In: Boyer, P.D. (Ed.): The Enzymes, 3rd Ed., Vol.4, pp. 337. New York: Academic Press 1971

    Google Scholar 

  • Edwards, M.J., Maguire, M.H.: Purification and properties of rat heart 5′-nucleotidase. Molec. Pharmacol. 6, 641–648 (1970)

    CAS  Google Scholar 

  • Edwards, N.L., Gelfand, E.W., Biggar, D., Fox, I.H.: Partial deficiency of purine nucleoside Phosphorylase studies of pruine and pyrimidine metabolism. J. Lab. Clin. Med. (In press) (1978)

    Google Scholar 

  • Edwards, Y.H., Edwards, P.A., Hopkinson, D.A.: A trimeric structure for mammalian purine nucleoside Phosphorylase. FEBS Letters 32, 235–237 (1973)

    PubMed  CAS  Google Scholar 

  • Edwards, Y.H., Hopkinson, D. A., Harris, H.: Inherited variants of human nucleoside Phosphorylase. Ann. hum. Genet. 34, 395–408 (1971)

    PubMed  CAS  Google Scholar 

  • Edwards, Y.H., Hopkinson, D.A., Harris, H.: Adenosine isozymes in human tissues. Ann. hum. Genet. 35, 207–219 (1971a)

    PubMed  CAS  Google Scholar 

  • Ernster, L., Jones, L.C.: A study of the nucleoside: Tri- and diphosphate activities of rat liver microsomes. J. Cell Biol. 15, 563–578 (1962)

    PubMed  CAS  Google Scholar 

  • Evans, W.H.: Nucleotide pyrophosphatase, a sialoglycoprotein located on the hepatocyte surface. Nature (Lond.) 250, 391–394 (1974)

    CAS  Google Scholar 

  • Evans, W.H., Gurd, J. W.: Properties of a 5′-nucleotidase purified from mouse liver plasma membranes. Biochem. J. 133, 189–199 (1973)

    PubMed  CAS  Google Scholar 

  • Farkas, W.R., Singh, R.D.: Guanine aminohydrolase in rate and mouse red cells: a potent inhibitor of guanylation of tRNA. Biochem. Biophys. Acta 377, 166–173 (1975)

    PubMed  CAS  Google Scholar 

  • Farquhar, M.G., Bergeron, J.J.M., Palade, G.E.: Cytochemistry of golgi fractions prepared from rat liver. J. Cell Biol. 60, 8–25 (1974)

    PubMed  CAS  Google Scholar 

  • Felicioli, R.A., Senesi, S., Marmocchi, F., Falcon, G., Ipata, P.L.: Nucleoside phosphomonoesterases during growth cycle of Bacillus subtilis. Biochemistry 12, 547–522 (1973)

    PubMed  CAS  Google Scholar 

  • Fischer, D., Van der Weyden, M.D., Snyderman, R., Kelley, W.N.: A role for adenosine deaminase in human monocyte maturation. J. clin. Invest. 58, 399–407 (1976)

    PubMed  CAS  Google Scholar 

  • Foltinova, I., Kuzela, S.: Effect of nucleosides on the synthesis of nucleic acids and proteins in Ehrlich ascites carcinoma cells. Neoplasma 23, 223–226 (1976)

    PubMed  CAS  Google Scholar 

  • Fox, I.H.: Human purine ribonucleotide catabolism clinical and biochemical significance. Nutr. Metab. 16, 79–86 (1974)

    Google Scholar 

  • Fox, I.H., Andres, C.M., Gelfand, E.W., Biggar, D.: Purine nucleoside Phosphorylase deficiency: altered kinetic properties of a mutant enzyme. Science 197, 1084–1086 (1977)

    PubMed  CAS  Google Scholar 

  • Fox, I.H., Kelley, W.N.: Phosphoribosylpyrophosphate in man: biochemical and clinical significance. Ann. intern. Med. 74, 424–433 (1971)

    PubMed  CAS  Google Scholar 

  • Fox, I.H., Kelley, W.N.: Studies on the mechanism of fructose-induced hyperuricemia in man. Metabolism 21, 713–721 (1972)

    PubMed  CAS  Google Scholar 

  • Fox, I.H., Keystone, E.C., Gladman, D.D., Moore, M., Cane, D.: Inhibition of mitogen mediated lymphocyte blastogenesis by adenosine. Immun. Commun. 4, 419–427 (1975)

    CAS  Google Scholar 

  • Fox, I.H., Marchant, P.J.: Human purine ribonucleotide catabolism: characterization of placental microsomal 5′-phosphomonoesterase. Can. J. Biochem. 54, 462–469 (1976)

    PubMed  CAS  Google Scholar 

  • Fox, I.H., Marchant, P.J.: Purine catabolism in man: inhibition of 5′-phosphomonoesterase activities from placental microsomes. Canad. J. Biochem. 54, 1055–1060 (1976a)

    CAS  Google Scholar 

  • Galanti, B., Russo, M., Nardiello, S., Giusti, G.: Activation energy, relative substrate specificity and optimum pH of guanase from human, rat mouse and guinea pig sera and tissues. Enzyme 20, 90–97(1975)

    PubMed  CAS  Google Scholar 

  • Galanti, B., Russo, M., Nardiello, S., Giusti, G.: Further observations on the properties of serum and tissue guanase from man and some animal species. Enzyme 21, 342–348 (1976)

    PubMed  CAS  Google Scholar 

  • George, D.L., Francke, U.: Gene dose effect: regional mapping of human nucleoside Phosphorylase on chromosome 14. Science 194, 851–852 (1976)

    PubMed  CAS  Google Scholar 

  • Giblett, E.R., Amman, A.J., Sandman, R., Wara, D.W., Diamond, L.K.: Nucleoside Phosphorylase deficiency in a child with severely defective T-cell immunity and normal B-cell immunity. Lancet 1975I, 1010–1013

    Google Scholar 

  • Giblett, E.R., Anderson, J. E., Cohen, F., Pollara, B., Meuwissen, H.J.: Adenosine deaminase deficiency in two patients with severely impaired cellular immunity. Lancet 1972II, 1067–1069

    Google Scholar 

  • Green, H., Chan, T.: Pyrimidine starvation induced by adenosine in fibroblasts and lymphoid cells: role of adenosine deaminase. Science 182, 836–837 (1973)

    PubMed  CAS  Google Scholar 

  • Grummt, F., Speckbacher, M.: GTP degradation to guanine catalyzed by ribosomal subunits and microsomal wash factors. Europ. J. Biochem. 57, 579–585 (1975)

    PubMed  CAS  Google Scholar 

  • Hardonk, M.J., DeBoer, H.G.A.: 5′-nucleotidase. III. Determinations of 5′-nucleotidase isozymes in tissues of rat and mouse. Histochimie 12, 29–41 (1968)

    PubMed  CAS  Google Scholar 

  • Hardonk, M.J., Koudstaal, J.: 5′-nucleotidase. II. The significance of 5′-nucleotidase in the metabolism of nucleotides studied by histochemical and biochemical techniques. Histochimie 12, 18–28(1968)

    PubMed  CAS  Google Scholar 

  • Henderson, J.F., Rosenbloom, F.M., Kelley, W.N., Seegmiller, J.E.: Variations in purine metabolism of cultured skin fibroblasts. J. clin. Invest. 47, 1511–1516 (1968)

    PubMed  CAS  Google Scholar 

  • Hirsch, J., Martelo, O.J.: Inhibition of nuclear protein kinases by adenosine analogues. Life Sci. 19, 85–90 (1976)

    PubMed  CAS  Google Scholar 

  • Hirschhorn, R.: Conversion of human erythrocyte-adenosine deaminase activity to different tissue-specific isozymes: evidence for a common catalytic unit. J. clin. Invest. 55, 661–667 (1975)

    PubMed  CAS  Google Scholar 

  • Hirschhorn, R., Bertatis, N., Rosen, F.S.: Characterization of residual enzyme activity in fibroblasts from patients with adenosine deaminase deficiency and combined immunodeficiency: evidence for a mutant enzyme. Proc. nat. Acad. Sci. (Wash.) 73, 213–217 (1976)

    CAS  Google Scholar 

  • Hirschhorn, R., Levytska, V., Pollara, B., Meuwissen, H.J.: Evidence for control of several different tissue-specific isoenzymes of adenosine deaminase by a single genetic locus. Nature (Lond.) New Biol. 246, 200–202 (1973)

    CAS  Google Scholar 

  • Hopkinson, D.A., Cook, P.J.L., Harris, H.: Further data on the adenosine deaminase (ADA) polymorphism and a report of a new phenotype. Ann. hum. Genet. 32, 361–367 (1969)

    PubMed  CAS  Google Scholar 

  • Hovi, T., Smyth, J.F., Allison, A.C., Williams, S.C.: Role of adenosine deaminase in lymphocyte proliferation. Clin. exp. Immunol. 23, 395–403 (1976)

    PubMed  CAS  Google Scholar 

  • Huang, C.M., Keenan, T.W.: Preparation and properties of 5′-nucleotidase from bovine milk fat globule membranes. Biochim. biophys. Acta (Amst.) 274, 246–257 (1972)

    CAS  Google Scholar 

  • Ipata, P.L.: Sheep brain 5′-nucleotidase. Some enzymatic properties and allosteric inhibition by nucleoside triphosphates. Biochemistry 7, 507–515 (1968)

    PubMed  CAS  Google Scholar 

  • Ischii, K., Green, H.: Lethality of adenosine for cultured mammalian cells by interference with pyrimidine biosynthesis. J. Cell Sci. 13, 429–439 (1973)

    Google Scholar 

  • Itoh, R., Mitsui, A., Tsushima, K.: 5′-nucleotidase of chicken liver. Biochim. biophys. Acta (Amst.) 146, 151–159(1967)

    CAS  Google Scholar 

  • Jensen, K.F., Nygaard, R: Purine nucleoside Phosphorylase from Escherichia coli and Salmonella typhimurium. Europ. J. Biochem. 51, 253–265 (1975)

    PubMed  CAS  Google Scholar 

  • Johnson, S.M., Asherson, G.L., Watts, R.W.E., North, M.E., Allsop, J., Webster, A.D.B.: Lymphocyte purine 5′-nucleotidase deficiency in primary hypogammaglobulinemia. Lancet 1977I, 168–170

    Google Scholar 

  • Josan, V., Krishman, P.S.: Regulation of rat liver guanine amino hydrolase by GTP. Biochem. Biophys. Res. Commun. 31, 299–302 (1968)

    CAS  Google Scholar 

  • Kanda, M., Brady, F.O., Rajagopalan, K.V., Handler, P.: Studies on the dissociation of flavin adenine dinucleotide from metalloflavoproteins. J. biol. Chem. 247, 765–770 (1972)

    PubMed  CAS  Google Scholar 

  • Kanda, M., Rajagopalan, K.V.: Nonequivalence of the flavin adenine dinucleotide moieties of chicken liver xanthine dehydrogenase. J. biol. Chem. 247, 2177–2182 (1972)

    PubMed  CAS  Google Scholar 

  • Kelley, W.N., Rosenbloom, F.M., Henderson, J.F., Seegmiller, J.E.: A specific enzyme defect in gout associated with overproduction of uric acid. Proc. nat. Acad. Sci. (Wash.) 57, 1735 – 1739(1967)

    CAS  Google Scholar 

  • Kim, B.K., Cha, S., Parks, Jr., R.E.: Purine nucleoside Phosphorylase from human erythrocytes. I. Kinetic analysis and substrate-binding studies. J. biol. Chem. 243, 1771–1776 (1968)

    PubMed  CAS  Google Scholar 

  • Knochel, J.P., Dotin, L.N., Hamburger, R.: Heat stress, exercise and muscle injury: effects on urate metabolism and renal function. Ann. intern. Med. 81, 321–328 (1974)

    PubMed  CAS  Google Scholar 

  • Krenitsky, T.A., Elion, G.B., Henderson, A.M., Hitchings, G.H.: Inhibition of human purine nucleoside Phosphorylase: studies with intact erythrocytes and the purified enzyme. J. biol. Chem. 243, 2876–2881 (1968)

    PubMed  CAS  Google Scholar 

  • Krenitsky, T.A., Neil, S.M., Elion, G.B., Hitchings, G.H.: A comparison of the specificities of xanthine oxidase and aldehyde oxidase. Arch. Biochem. Biophys. 150, 585–599 (1972)

    PubMed  CAS  Google Scholar 

  • Kumar, S., Josan, V., Sanger, K.C.S., Tewari, K.K., Krishnan, P.S.: Studies on guanine deaminase and its inhibitors in rat tissues. Biochem. J. 102, 691–704 (1967)

    PubMed  CAS  Google Scholar 

  • Kumar, K.S., Sitaramayya, A., Krishnan, P.S.: Guanine deaminase in rat liver and mouse liver and brain. Biochem. J. 128, 1079–1088 (1972)

    PubMed  CAS  Google Scholar 

  • Kumar, K.S., Sitaramayya, A., Krishnan, P.S.: Modulation of guanine deaminase. Biochem. J. 131,683–687(1973)

    PubMed  CAS  Google Scholar 

  • Kuriyama, Y.: Studies on microsomal nucleoside diphosphatase of rat hepatocytes. J. biol. Chem. 247, 2979–2988 (1972)

    PubMed  CAS  Google Scholar 

  • Lacroix, S., Moore, M., Fox, I.H.: (unpublished observations)

    Google Scholar 

  • Lalanne, M., Willemot, J.: Xanthine oxidase from mouse skeletal muscle purification and kinetic studies. Int. J. Biochem. 6, 479–484 (1975)

    CAS  Google Scholar 

  • Levin, S.J., Bodansky, O.: The double pH optimum of 5′-nucleotidase of bull seminal plasma. J. biol. Chem. 241, 51–56 (1966)

    PubMed  CAS  Google Scholar 

  • Lewis, A.S., Glantz, M.D.: Rabbit liver guanine deaminase: chemical, physical, and kinetic properties. J. biol. Chem. 249, 3862–3866 (1974)

    PubMed  CAS  Google Scholar 

  • Lewis, A.S., Glantz, M.D.: Isolation and purification of rabbit liver guanine deaminase. J. biol. Chem. 250, 8220–8221 (1975)

    PubMed  CAS  Google Scholar 

  • Lewis, A.S., Glantz, M.D.: Monomeric purine nucleoside Phosphorylase from rabbit liver: purification and characterization. J. biol. Chem. 251, 407–413 (1976)

    PubMed  CAS  Google Scholar 

  • Li, C., Hochstadt, J.: Transport mechanisms in isolated plasma membranes: nucleoside processing by membrane vesicles from mouse fibroblast cells grown in defined medium. J. biol. Chem. 251, 1175–1180 (1976)

    PubMed  CAS  Google Scholar 

  • Lisowski, J.: 5′-nucleotide phosphohydrolase from bovine pituitary gland. Biochim. biophys. Acta (Amst.) 113, 321–331 (1966)

    CAS  Google Scholar 

  • Lomax, C.A., Bagnara, A.S., Henderson, J.F.: Studies of regulation of purine nucleotide catabo-lism. Canad. J. Biochem. 53, 231–241 (1975)

    CAS  Google Scholar 

  • Lomax, C.A., Henderson, J.F.: Adenosine formation and metabolism during adenosine triphosphate catabolism in Ehrlich ascites tumor cells. Cancer Res. 33, 2825–2829 (1973)

    PubMed  CAS  Google Scholar 

  • Lowry, O.H., Carter, J., Ward, J.B., Glaser, L.: The effects of carbon and nitrogen sources on the level of metabolic intermediates in Escherichia coli.J. biol. Chem. 246, 6511–6521 (1971)

    PubMed  CAS  Google Scholar 

  • Lowry, O.H., Passonneau, J.V., Hasselberger, F.X., Schultz, D.W.: The relationship between substrates and enzymes of glycosine in brain. J. biol. Chem. 239, 18–30 (1964)

    PubMed  CAS  Google Scholar 

  • Maenpaa, P.H., Raivio, K.O., Kekomaki, M.P.: Liver adenine nucleotides; fructose-induced depletion and its effect on protein synthesis. Science 161, 1253–1255 (1968)

    PubMed  CAS  Google Scholar 

  • Maguire, M.H., Sim, M.K.: Studies on adenosine deaminase 2. specificity and mechanism of action of bovine placental adenosine deaminase. Europ. J. Biochem. 23, 22–29 (1971)

    PubMed  CAS  Google Scholar 

  • Mandel, H.G., Way, J.L., Smith, P.K.: The effect of 4-amino-5-imidazolecarboxamide on the incorporation of purines into liver nucleic acids of the mouse. Biochim. biophys. Acta (Amst.) 23, 402–404(1957)

    CAS  Google Scholar 

  • Mansoor, M., Kalyankar, G.D., Talwar, G.P.: Brain guanine deaminase: purification properties and regional distribution. Biochim. biophys. Acta (Amst.) 77,307–317 (1963)

    CAS  Google Scholar 

  • Marcolongo, R., Marinello, E., Pompucci, G., Pagani, R.: The role of xanthine oxidase in hyperuricemic states. Arthr. and Rheum. 17, 430–438 (1974)

    CAS  Google Scholar 

  • Marx, J.L.: Cyclic AMP in brain: role in synaptic transmission. Science 178, 1188–1190 (1972)

    PubMed  CAS  Google Scholar 

  • Matsuzaki, S., Pochet, R., Schell-Frederick, E.: A comparison of the subcellular distribution of 5′-nucleotidase, (Na+-K+)-ATP’ase and adenyl cyclase in beef thyroid gland. Biochim. biophys. Acta (Amst.) 313, 329–337 (1973)

    CAS  Google Scholar 

  • McComb, R.B., Yushok, W.D.: Metabolism of ascites tumor cells. IV. Enzymatic reaction involved in adenosine triphosphate degradation induced by 2-deoxyglucose. Cancer Res. 24, 198–203 (1964)

    PubMed  CAS  Google Scholar 

  • Meuwissen, H.J., Pickering, R.J., Pollara, B., Porter, I.H.: Combined immunodeficiency disease and adenosine deaminase deficiency: a molecular defect. New York: Academic Press 1975

    Google Scholar 

  • Mills, G.C., Schmalstieg, F.C., Trimmer, K.B., Goldman, A.S., Goldblum, R.M.: Purine metabolism in adenosine deaminase deficiency. Proc. nat. Acad. Sci. (Wash.) 73, 2867–2871 (1976)

    CAS  Google Scholar 

  • Milman, G., Anton, D.L., Weber, J.L.: Chinese hamster purine-nucleoside Phosphorylase: purification, structural, and catalytic properties. Biochemistry 15, 4967–4973 (1976)

    PubMed  CAS  Google Scholar 

  • Moir, T.W., Downs, T.D.: Myocardial reactive hyperemia: comparative effects of adenosine, ATP, ADP, AMP. Amer. J. Physiol. 222, 1386–1390 (1972)

    PubMed  CAS  Google Scholar 

  • Murakami, K., Tsushima, K.: Crystallization and some properties of purine nucleoside Phosphorylase from chicken liver. Biochim. biophys. Acta (Amst.) 384, 390–398 (1975)

    CAS  Google Scholar 

  • Murray, A.W.: Some properties of adenosine kinase from Ehrlich ascites tumour cells. Biochem. J. 106, 549–555 (1968)

    PubMed  CAS  Google Scholar 

  • Murray, A. W., Friedrichs, B.: Inhibition of 5′-nucleotidase from Ehrlich ascites tumour cells by nucleoside triphosphates. Biochem. J. 111, 83–89 (1969)

    PubMed  CAS  Google Scholar 

  • Nagler, L.G., Vartanyan, L.S.: Subunit structure of bovine milk xanthine oxidase: effect of limited cleavage by proteolytic enzymes on activity and structure. Biochim. biophys. Acta (Amst.) 427, 78–90(1976)

    CAS  Google Scholar 

  • Naito, Y., Tsushima, K.: Cytosol 5′-nucleotidase from chicken liver. Biochim. biophys. Acta (Amst.) 438, 159–168 (1976)

    CAS  Google Scholar 

  • Nakamura, S.: Effect of sodium deoxycholate on 5′-nucleotidase. Biochim. biophys. Acta (Amst.) 426, 339–347 (1976)

    CAS  Google Scholar 

  • Narins, R.G., Weisberg, J.S., Meyers, A.R.: Effects of carbohydrate on uric acid metabolism. Metabolism 23, 455–465 (1974)

    PubMed  CAS  Google Scholar 

  • Neu, H.C.: The 5′-nucleotidase of Escherichia coli. I. Purification and properties. J. biol. Chem. 242, 3896–3904(1967)

    PubMed  CAS  Google Scholar 

  • Neu, H.C.: The 5′-nucleotidase of Escherichia coli. II. Surface localization and purification of the E. coli 5′-nucleotidase inhibitor. J. biol. Chem. 242, 3905–3911 (1967a)

    PubMed  CAS  Google Scholar 

  • Neu, H.C.: The 5′-nucleotidase (uridine diphosphate sugar hydrolases) of the enterobacteriacea. Biochemistry 7, 3766–3773 (1968)

    PubMed  CAS  Google Scholar 

  • Newly, A.C., Luzio, J.P., Hales, C.N.: The properties and extracellular location of 5′-nucleotidase of the rat fat-cell plasma membrane. Biochem. J. 146, 625–633 (1975)

    Google Scholar 

  • Nishihara, H., Ishikawa, S., Shinkai, K., Akedo, H.: Multiple forms of human adenosine deaminase. II. Isolation and properties of a conversion factor from human lung. Biochim. biophys. Acta (Amst.) 302, 429–442 (1972)

    Google Scholar 

  • Osborne, W.R. A., Spencer, N.: Partial purification and properties of the common inherited forms of adenosine deaminase from human erythrocytes. Biochem. J. 133, 117–123 (1973)

    PubMed  CAS  Google Scholar 

  • Overgaard-Hansen, K.: Metabolic regulation of the adenine nucleotide pool I. studies on the transient exhaustion of the adenine nucleotides by glucose in Ehrlich ascites tumor cells. Biochim. biophys. Acta (Amst.) 104, 330–347 (1965)

    CAS  Google Scholar 

  • Parks Jr., R.E.: Discussion in Combined Immunodeficiency Disease and Adenosine Deaminase Deficiency: a Molecular Defect, pp. 195–199. In: Meuwissen, H.J., Pickering, R.J., Pollara, B., Porter, I.H. (Eds.). New York: Academic Press 1975

    Google Scholar 

  • Perheentupa, J., Raivio, K.: Fructose-induced hyperuricemia. Lancet 1967II, 528–531

    Google Scholar 

  • Pfrogner, N.: Adenosine deaminase from calf spleen. I. Purification. Arch. Biochem. Biophys. 119, 141–146(1967)

    Google Scholar 

  • Pfrogner, N.: Adenosine deaminase from calf spleen. II. Chemical and enzymological properties. Arch. Biochem. Biophys. 119, 147–154 (1967a)

    PubMed  CAS  Google Scholar 

  • Pierre, J.W. de, Karnovsky, M.L.: Ecto-enzyme of granulocytes: 5′-nucleotidase. Science 183, 1096–1098 (1974)

    Google Scholar 

  • Piggott, C.O., Brady, T.G.: Purification of multiple forms of adenosine deaminase from rabbit intestine. Biochim. biophys. Acta (Amst.) 429, 600–607 (1976)

    CAS  Google Scholar 

  • Pinsley, C.L., Scruton, M.C.: Nucleoside dephosphatase from pig liver, purification and some properties. Arch. Biochem. Biophys. 158, 331–345 (1973)

    PubMed  CAS  Google Scholar 

  • Planet, G., Fox, I.H.: Inhibition of phosphoribosylpyrophosphate synthesis by purine nucleosides in human erythrocytes. J. biol. Chem. 251, 5839–5844 (1976)

    PubMed  CAS  Google Scholar 

  • Planet, G., Fox, I.H.: Inhibition of pyrimidine nucleotide biosynthesis by purine nucleosides in human cells, (in preparation)

    Google Scholar 

  • Pletsch, Q.A., Coffey, J.W.: Studies on 5′-nucleotidases of rat liver. Biochim. biophys. Acta (Amst.) 276, 192–205 (1972)

    CAS  Google Scholar 

  • Polmar, S.H., Stern, R.C., Schwartz, A.L., Wetzler, E.M., Chase, P.A., Hirschhorn, R.: Enzyme replacement therapy for adenosine deaminase deficiency and severe combined immunodeficiency. New Engl. J. Med. 295, 1337–1343 (1976)

    PubMed  CAS  Google Scholar 

  • Prajda, N., Weber, G.: Malignant transformation linked inbalance: decreased xanthine oxidase activity in hepatomas. FEBS. Letters 59, 245–249 (1975)

    PubMed  CAS  Google Scholar 

  • Raivio, K.O., Becker, M. A., Meyer, L.J., Greene, M.L., Nuki, G., Seegmiller, J.E.: Stimulation of human purine synthesis de novo by fructose infusion. Metabolism 24, 861–869 (1975)

    PubMed  CAS  Google Scholar 

  • Rakestraw, N.W.: Chemical factors in fatigue. I. The effects of muscular exercise upon certain common blood constituents. J. biol. Chem. 47, 565–591 (1921)

    CAS  Google Scholar 

  • Reimer, B.L., Widnell, C.C.: The demonstration of a specific 5′-nucleotidase activity in rat tissues. Arch. Biochem. Biophys. 171, 343–347 (1975)

    Google Scholar 

  • Robertson, B.C., Hoffee, P.A.: Purification and properties of purine nucleoside Phosphorylase from Salmonella typhimurium. J. biol. Chem. 248, 2040–2043 (1973)

    PubMed  CAS  Google Scholar 

  • Rossi, C.A., Lucacchini, A., Montali, U., Ronca, G.: A general method of purification of adenosine deaminase by affinity chomatography. Int. J. Pept. Protein Res. 7, 81–89 (1975)

    PubMed  CAS  Google Scholar 

  • Rowe, P.B., Wyngaarden, J.B.: The mechanism of dietary alterations in rat hepatic xanthine oxidase levels. J. biol. Chem. 241, 5571–5576 (1966)

    PubMed  CAS  Google Scholar 

  • Rubio, R., Berne, R. M.: Release of adenosine by normal myocardium in dogs and its relationship to regulation of coronary resistance. Circulat. Res. 25,407–415 (1969)

    PubMed  CAS  Google Scholar 

  • Rubio, R., Berne, R.M., Katori, M.: Release of adenosine in reactive hyperemia of the dog heart. Amer. J. Physiol. 216, 56–62 (1969)

    PubMed  CAS  Google Scholar 

  • Rubio, V.R., Weidmeier, T., Berne, R.M.: Nucleoside Phosphorylase: location and role in the myocardial distribution of purines. Amer. J. Physiol. 222, 550–555 (1972)

    PubMed  CAS  Google Scholar 

  • Satchell, D.G., Maguire, M.H.: Inhibitory effects of adenine nucleotide analogs on the isolated guinea pig taenia coli. J. Pharmacol, exp. Ther. 195, 540–548 (1975)

    CAS  Google Scholar 

  • Schrader, W.P., Stacy, A.R., Pollara, B.: Purification of human erythrocyte adenosine deaminase by affinity column chromatography. J. biol. Chem. 251, 4026–4032 (1976)

    PubMed  CAS  Google Scholar 

  • Scott, T.G.: The distribution of 5′-nucleotidase in the brain of the mouse. J. Histochem. Cytochem. 13, 657–667(1965)

    PubMed  CAS  Google Scholar 

  • Sim, M.K., Maguire, M.H.: Studies on adenosine deaminase. I. Purification and some properties of bovine placental adenosine deaminase. Eur. J. Biochem. 23, 17–21 (1971)

    PubMed  CAS  Google Scholar 

  • Simkin, P.A.: Hexose infusions in Cebus monkeys: effects on uric acid metabolism. Metabolism 21, 1029–1036 (1972)

    PubMed  CAS  Google Scholar 

  • Sitaramayya, A., Ali, S., Kumar, K.S., Krishnan, P.S.: Induction of guanine deaminase and its inhibitor in rodent liver and brain. Biochem. J. 138, 143–146 (1974)

    PubMed  CAS  Google Scholar 

  • Sitaramayya, A., Kumar, K.S., Krishnan, P.S.: Isoenzymicity in mouse liver guanine deaminase demonstrable under substrate stress. Biochem. Biophys. Res. Commun. 70, 480–484 (1976)

    PubMed  CAS  Google Scholar 

  • Smythe, H.A.: Xanthine and uric acid as xanthine oxidase inhibitors. Arthr. and Rheum. 20, 135–136(1977)

    Google Scholar 

  • Snyder, F.F., Mendelsohn, J., Seegmiller, J.E.: Adenosine metabolism in phytohemagglutinin-stimulated human lymphocytes. J. clin. Invest. 58, 654–666 (1976)

    PubMed  CAS  Google Scholar 

  • Soder, C., Henderson, J.F., Zombor, G., McCoy, E.E., Verhoef, V., Morris, A.J.: Relationship between nucleoside triphosphate pyrophosphohyrolase activity and inosine triphosphate accumulation in human erythrocytes. Canad. J. Biochem. 54, 843–847 (1976)

    CAS  Google Scholar 

  • Solyom, A., Trams, E.G.: Enzyme markers in characterization of isolated plasma membranes. Enzyme 13, 329–372(1972)

    PubMed  CAS  Google Scholar 

  • Song, C. S., Bodansky, O.: Purification of 5′-nucleotidase from human liver. Biochem. J. 101, 5 c— 6 c (1966)

    Google Scholar 

  • Song, C.S., Bodansky, D.: Subcellular localization and properties of 5′-nucleotidase in the rat liver. J. biol. Chem. 242, 694–699 (1967)

    PubMed  CAS  Google Scholar 

  • Stefanovic, V., Mandel, P., Rosenberg, A.: Concanavalin A inhibition of ecto-5′-nucleotidase of intact cultured C6 glioma cells. J. biol. Chem. 250, 7081–7083 (1975)

    PubMed  CAS  Google Scholar 

  • Sutton, J., Fox, LH.: Alterations in purine metabolism during strenuous musclar exercise in man. Clin. Res. 23, 639 A (1975)

    Google Scholar 

  • Tanaka, R., Morita, H., Teruya, A.: Isolation and properties of 5′-nucleotidase from a membrane fraction of bovine cerebral cortex. Biochim. biophys. Acta (Amst.) 298, 842–849 (1973)

    CAS  Google Scholar 

  • Tanaka, R., Teruya, A., Morita, H.: Effects of divalent cations on 5′-mononucleotidase of bovine cerebral cortex. Canad. J. Biochem. 51, 841–848 (1973a)

    CAS  Google Scholar 

  • Trams, E.G., Lauter, C.J.: Adenosine deaminase of cultured brain cells. Biochem. J. 152, 681–687 (1975)

    PubMed  CAS  Google Scholar 

  • Trotta, P.P., Smithwick, E.M., Balis, M.E.: A normal level of adenosine deaminase in red cell lysates of carriers and patients with severe combined immunodeficiency. Proc. nat. Acad. Sci. (Wash.) 73,104–108(1976)

    CAS  Google Scholar 

  • Ullman, B., Cohen, A., Martin Jr., D. W.: Characterization of a cell culture model for the study of adenosine deaminase and purine nucleoside phosphorylase-deficienct immunologic disease. Cell 9, 205–211 (1976)

    PubMed  CAS  Google Scholar 

  • Valentine, W.N., Paglia, D.E., Tartaglia, A.P., Gilsanz, F.: Hereditary hemolytic anemia with increased red cell adenosine deaminase (45- to 70-fold) and decreased adenosine triphosphate. Science 195, 783–785 (1977)

    PubMed  CAS  Google Scholar 

  • Van der Weyden, M.B., Buckley, R.H., Kelley, W.N.: Molecular form of adenosine deaminase in severe combined immunodeficiency. Biochem. Biophys. Res. Commun. 57, 590–595 (1974)

    PubMed  Google Scholar 

  • Van der Weyden, M.B., Kelley, W.N.: Catalytic and physical characteristics of adenosine deaminase in severe combined immunodeficiency. J. clin. Chem. Clin. Biochem. 14, 326–327 (1976)

    Google Scholar 

  • Van der Weyden, M.B., Kelley, W.N.: Human adenosine deaminase: distribution and properties. J. biol. Chem. 251, 5448–5456 (1976a)

    PubMed  Google Scholar 

  • Vornovitskaya, G.I., Ioannesyants, I.A., Borsenko, B.G., Shapot, V.S.: Effect of deoxyadenosine on the nucleic acids synthesis in malignant cells in the presence of an inhibitor of deaminase. Vaprosy Meditsinkoi 21, 192–194 (1975)

    CAS  Google Scholar 

  • Wadman, S.K., Bree, P.K.de, VanGennip, A.H., Stoop, J.W., Zegers, B.J.M., Staal, G.E.J., Siegenbeck, L.H.: Urinary purine in patients with a severely defective T-cell immunity and a purine nucleoside Phosphorylase deficiency in erythrocytes and lymphocytes. J. clin. Chem. Biochem. 14, 326 (1976)

    Google Scholar 

  • Wauld, W.R., Brady, F.O., Wiley, R.D., Rajagopalan, K.V.: A new purification procedure for bovine milk xanthine oxidase: effect of proteolysis on subunit structure. Arch. Biochem. Biophys. 169, 695–701 (1975)

    Google Scholar 

  • Wauld, W.R., Rajagopalan, K.V.: Purification and properties of the NAD +-dependent (TypeD) and O2-dependent (Type O) forms of rat liver xanthine dehydrogenase. Arch. Biochem. Biophys. 172, 354–364 (1976)

    Google Scholar 

  • Wauld, W.R., Rajagopalan, K. V.: The mechanism of conversion of rat liver xanthine dehydrogenase from an NAD+-dependent form (TypeD) to an O2-dependent form (TypeO). Arch. Biochem. Biophys. 172, 365–379 (1976a)

    Google Scholar 

  • Weston, A.H.: Nerve-mediated inhibition of mechanical activity in rabbit duodenum and the effects of desentization to adenosine and several of its derivatives. Brit. J. Pharmacol. 48, 302–308 (1973)

    CAS  Google Scholar 

  • Widnell, C.C.: Cytochemical localization of 5′-nucleotidase in subcellular fractions isolated from rat liver. I. The origin of 5′-nucleotidase activity in microsomes. J. Cell Biol. 52, 542–558 (1972)

    PubMed  CAS  Google Scholar 

  • Widnell, C.C., Unkeless, J.G: Partial purification of a lipoprotein with 5′-nucleotidase activity from membrane of rat liver cells. Proc. nat. Acad. Sci. (Wash.) 61, 1050–1057 (1968)

    CAS  Google Scholar 

  • Wolberg, G., Zimmerman, T.P., Hiemstra, K., Winston, M., Chu, L.: Adenosine inhibition of lymphocyte-mediated cytolysis: possible role of cyclic adenosine monophosphate. Science 187, 957–959(1975)

    PubMed  CAS  Google Scholar 

  • Wong, P.L.C., Henderson, J.F.: Purine ribonucleotide biosynthesis, interconversion and catabo-lism in mouse brain in vitro. Biochem. J. 129, 1085–1094 (1972)

    PubMed  CAS  Google Scholar 

  • Woo, Y., Manery, J.F.: 5′-nucleotidase: an ecto-enzyme of frog skeletal muscle. Biochim. Biophys. Acta (Wash.) 397, 144–152 (1975)

    CAS  Google Scholar 

  • Woods, H.F., Eggleston, L.V., Krebs, H.A.: The cause of hepatic accumulation of fructose-1-phosphate on fructose loading. Biochem. J. 119, 501–510 (1970)

    PubMed  CAS  Google Scholar 

  • Woodward, N.D., Lee, P.C., Delapp, N.W., Fisher, J.R.: Induction of chicken liver xanthine dehydrogenase by purines. Arch. Biochem. Biophys. 153, 537–542 (1972)

    PubMed  CAS  Google Scholar 

  • Wyngaarden, J.B.: Xanthinuria. In: Stanbury, J.B., Wyngaarden, J.B., Fredrickson, D.S. (Eds.): The Metabolic Basis of Inherited Disease, 3rd Ed. New York: McGraw-Hill 1972

    Google Scholar 

  • Wyngaarden, J.B., Kelley, W.N.: Gout and Hyperuricemia. New York: Grune and Stratton 1976

    Google Scholar 

  • Zenser, T.V.: Formation of adenosine 3′, 5′-monophosphate from adenosine in mouse thymocytes. Biochem. Biophys. Acta 404, 202–213 (1975)

    PubMed  CAS  Google Scholar 

  • Zielke, C.L., Suelter, C.H.: Purine, Purine Nucleoside, and Purine Nucleotide Aminohydrolases. In: Boyer, P.D. (Ed.); The Enzymes, 3rd Ed., Vol.4, pp. 47–48. New York: Academic Press 1971

    Google Scholar 

  • Zimmerman, M., Gersten, N., Miech, P.R.: Adenine and adenosine metabolism in liver. Proc. Amer. Ass. Cancer Res. 11, 87 (1970)

    Google Scholar 

  • Zimmerman, T.P., Rideout, J.L., Wolberg, G., Duncan, G.S., Elion, G.B.: 2-Fluoroadenosine 3′: 5′-monophosphate: a metabolite of 2-fluoroadenosine in mouse cytoxic lymphocytes. J. biol. Chem. 251, 6757–6766 (1976)

    PubMed  CAS  Google Scholar 

Download references

Authors
  1. I. H. Fox
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. Department of Internal Medicine, Medical School, University of Michigan, Ann Arbor, MI, 48109, USA

    William N. Kelley MD (Professor and Chairman) (Professor and Chairman)

  2. Department of Pathology, Upstate Medical Center, Syracuse, NY, 13210, USA

    Irwin M. Weiner MD (Professor and Chairman) (Professor and Chairman)

Rights and permissions

Reprints and permissions

Copyright information

© 1978 Springer-Verlag Berlin Heidelberg

About this chapter

Cite this chapter

Fox, I.H. (1978). Degradation of Purine Nucleotides. In: Kelley, W.N., Weiner, I.M. (eds) Uric Acid. Handbook of Experimental Pharmacology, vol 51. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-66867-8_5

Download citation

  • DOI: https://doi.org/10.1007/978-3-642-66867-8_5

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-66869-2

  • Online ISBN: 978-3-642-66867-8

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation