메뉴 건너뛰기




Volumn 67, Issue 2, 1996, Pages 795-804

A low-K(m) 5'-nucleotidase from rat brain cytosolic fraction: Purification, kinetic properties, and description of regulation by a novel factor that increases sensitivity to inhibition by ATP and ADP

Author keywords

5' Nucleotidase; Adenine nucleotides; Brain; Protein purification

Indexed keywords

5' NUCLEOTIDASE; ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; ALPHA,BETA METHYLENEADENOSINE DIPHOSPHATE; BRAIN ENZYME; PHOSPHATIDYLINOSITOL; PHOSPHOLIPASE C; ENZYME INHIBITOR;

EID: 0029665455     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1996.67020795.x     Document Type: Article
Times cited : (16)

References (70)
  • 1
    • 0021763832 scopus 로고
    • The existence and properties of two dimers of rat liver ecto-5′-nucleotidase
    • Bailyes E. M., Soos M., Jackson P., Newby A. C., Siddle K., and Luzio J. P. (1984) The existence and properties of two dimers of rat liver ecto-5′-nucleotidase. Biochem. J. 221, 369-377.
    • (1984) Biochem. J. , vol.221 , pp. 369-377
    • Bailyes, E.M.1    Soos, M.2    Jackson, P.3    Newby, A.C.4    Siddle, K.5    Luzio, J.P.6
  • 2
    • 0023078640 scopus 로고
    • The synthesis and turnover of 5′-nucleotidase in primary cultured hepatocytes
    • Baron M. D. and Luzio J. P. (1987) The synthesis and turnover of 5′-nucleotidase in primary cultured hepatocytes. Biochim. Biophys. Acta 927, 81-85.
    • (1987) Biochim. Biophys. Acta , vol.927 , pp. 81-85
    • Baron, M.D.1    Luzio, J.P.2
  • 3
    • 0016224631 scopus 로고
    • Release of adenosine from ischaemic brain. Effect of cerebral vascular resistance and incorporation into cerebral adenine nucleotides
    • Berne R. M., Rubio R., and Curnish R. R. (1974) Release of adenosine from ischaemic brain. Effect of cerebral vascular resistance and incorporation into cerebral adenine nucleotides. Circ. Res. 35, 262-271.
    • (1974) Circ. Res. , vol.35 , pp. 262-271
    • Berne, R.M.1    Rubio, R.2    Curnish, R.R.3
  • 4
    • 0024337483 scopus 로고
    • Stimulation by glycerate 2,3-bisphosphate: A common property of cytosolic IMP-GMP 5′-nucleotidase in rat and human tissues
    • Bontemps F., Vincent M. F., Van den Bergh F., van Waeg G., and Van den Bergh G. (1989) Stimulation by glycerate 2,3-bisphosphate: a common property of cytosolic IMP-GMP 5′-nucleotidase in rat and human tissues. Biochim. Biophys. Acta 997, 131-134.
    • (1989) Biochim. Biophys. Acta , vol.997 , pp. 131-134
    • Bontemps, F.1    Vincent, M.F.2    Van Den Bergh, F.3    Van Waeg, G.4    Van Den Bergh, G.5
  • 5
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier C. (1981) Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem. 256, 1604-1607.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 6
    • 0024592380 scopus 로고
    • Human placental ecto-5′-nucleotidase: Isoforms and chemical crosslinking products of the membrane-bound and isolated enzyme
    • Buschette-Brambrink S. and Gutensohn W. (1989) Human placental ecto-5′-nucleotidase: isoforms and chemical crosslinking products of the membrane-bound and isolated enzyme. Biol. Chem. Hoppe Seyler 370, 67-74.
    • (1989) Biol. Chem. Hoppe Seyler , vol.370 , pp. 67-74
    • Buschette-Brambrink, S.1    Gutensohn, W.2
  • 7
    • 4244120872 scopus 로고
    • Microdetermination of phosphorous
    • Chen P. S., Toribara T. Y., and Warner H. (1956) Microdetermination of phosphorous. Anal. Chem. 28, 1756-1758.
    • (1956) Anal. Chem. , vol.28 , pp. 1756-1758
    • Chen, P.S.1    Toribara, T.Y.2    Warner, H.3
  • 8
    • 0015972948 scopus 로고
    • A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors
    • Cornish-Bowden A. (1974) A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors. Biochem. J. 137, 143-144.
    • (1974) Biochem. J. , vol.137 , pp. 143-144
    • Cornish-Bowden, A.1
  • 9
    • 0023162442 scopus 로고
    • 2 adenosine receptors in spinal mechanisms of antinociception
    • 2 adenosine receptors in spinal mechanisms of antinociception. Eur. J. Pharmacol. 139, 215-223.
    • (1987) Eur. J. Pharmacol. , vol.139 , pp. 215-223
    • De Lander, G.E.1    Hopkins, C.J.2
  • 11
    • 0023280998 scopus 로고
    • 8-Cyclopentyl-1,3-dimethylxanthine prolongs epileptic seizures in rats
    • Dragunow M. and Robertson H. A. (1987) 8-Cyclopentyl-1,3-dimethylxanthine prolongs epileptic seizures in rats. Brain Res. 417, 377-379.
    • (1987) Brain Res. , vol.417 , pp. 377-379
    • Dragunow, M.1    Robertson, H.A.2
  • 12
    • 0022361353 scopus 로고
    • Is adenosine an endogenous anticonvulsant?
    • Dragunow M., Goddard G. V., and Laverty R. (1985) Is adenosine an endogenous anticonvulsant? Epilepsia 26, 480-487.
    • (1985) Epilepsia , vol.26 , pp. 480-487
    • Dragunow, M.1    Goddard, G.V.2    Laverty, R.3
  • 13
    • 0020072995 scopus 로고
    • Sedative and anticonvulsant effects of adenosine analogues in the mouse and rat
    • Dunwiddie T. V. and Worth T. (1982) Sedative and anticonvulsant effects of adenosine analogues in the mouse and rat. J. Pharmacol. Exp. Ther. 220, 70-76.
    • (1982) J. Pharmacol. Exp. Ther. , vol.220 , pp. 70-76
    • Dunwiddie, T.V.1    Worth, T.2
  • 14
    • 0023882404 scopus 로고
    • How does adenosine inhibit transmitter release?
    • Fredholm B. B. and Dunwiddie T. V. (1988) How does adenosine inhibit transmitter release? Trends Pharmacol. Sci. 9, 130-134.
    • (1988) Trends Pharmacol. Sci. , vol.9 , pp. 130-134
    • Fredholm, B.B.1    Dunwiddie, T.V.2
  • 15
    • 0014976981 scopus 로고
    • Synaptic vesicles in sympathetic neurons
    • Geffen L. B. and Livett B. G. (1971) Synaptic vesicles in sympathetic neurons. Physiol. Rev. 51, 98-157.
    • (1971) Physiol. Rev. , vol.51 , pp. 98-157
    • Geffen, L.B.1    Livett, B.G.2
  • 16
    • 0023030975 scopus 로고
    • The hydrolysis of extracellular adenine nucleotides by cultured endothelial cells from pig aorta. Feed-forward inhibition of adenosine production at the cell surface
    • Gordon E. L., Pearson J. D., and Slakey L. L. (1986) The hydrolysis of extracellular adenine nucleotides by cultured endothelial cells from pig aorta. Feed-forward inhibition of adenosine production at the cell surface. J. Biol. Chem. 261, 15496-15504.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15496-15504
    • Gordon, E.L.1    Pearson, J.D.2    Slakey, L.L.3
  • 17
    • 0021009420 scopus 로고
    • Purification and properties of bovine liver plasma membrane 5′-nucleotidase
    • Harb J., Meflah K., Duflos Y., and Bernard S. (1983) Purification and properties of bovine liver plasma membrane 5′-nucleotidase. Eur. J. Biochem. 137, 131-138.
    • (1983) Eur. J. Biochem. , vol.137 , pp. 131-138
    • Harb, J.1    Meflah, K.2    Duflos, Y.3    Bernard, S.4
  • 18
    • 0002975564 scopus 로고
    • ATP receptors and their physiological roles
    • (Stone T. W., ed.), Academic Press, London
    • Hoyle C. H. V. and Burnstock G. (1991) ATP receptors and their physiological roles, in Adenosine in the Nervous System (Stone T. W., ed.), pp. 44-76, Academic Press, London.
    • (1991) Adenosine in the Nervous System , pp. 44-76
    • Hoyle, C.H.V.1    Burnstock, G.2
  • 19
    • 0027393389 scopus 로고
    • Production of adenosine from extracellular ATP at the striatal cholinergic synapse
    • James S. and Richardson P. J. (1993) Production of adenosine from extracellular ATP at the striatal cholinergic synapse. J. Neurochem. 60, 219-227.
    • (1993) J. Neurochem. , vol.60 , pp. 219-227
    • James, S.1    Richardson, P.J.2
  • 20
    • 0021995860 scopus 로고
    • Release of purines, noradrenaline, and GABA from rat hippocampal slices by field stimulation
    • Jonzon B. and Fredholm B. B. (1985) Release of purines, noradrenaline, and GABA from rat hippocampal slices by field stimulation. J. Neurochem. 44, 217-224.
    • (1985) J. Neurochem. , vol.44 , pp. 217-224
    • Jonzon, B.1    Fredholm, B.B.2
  • 22
    • 0015003286 scopus 로고
    • Isolation and characterization of sympathetic nerve trunk vesicles
    • Lagercrantz H. (1971) Isolation and characterization of sympathetic nerve trunk vesicles. Acta Physiol. Scand. Suppl. 366, 1-44.
    • (1971) Acta Physiol. Scand. Suppl. , vol.366 , pp. 1-44
    • Lagercrantz, H.1
  • 23
    • 0025910513 scopus 로고
    • A comparison of the properties of 5′-nucleotidase purified from the cytosolic and synaptic plasma membrane fractions of rat forebrain
    • Lai K.-M. and Wong P. C. L. (1991a) A comparison of the properties of 5′-nucleotidase purified from the cytosolic and synaptic plasma membrane fractions of rat forebrain. Int. J. Biochem. 23, 1123-1130.
    • (1991) Int. J. Biochem. , vol.23 , pp. 1123-1130
    • Lai, K.-M.1    Wong, P.C.L.2
  • 24
    • 0025940228 scopus 로고
    • Metabolism of extracellular adenine nucleotides by cultured rat brain astrocytes
    • Lai K.-M. and Wong P. C. L. (1991b) Metabolism of extracellular adenine nucleotides by cultured rat brain astrocytes. J. Neurochem. 57, 1510-1515.
    • (1991) J. Neurochem. , vol.57 , pp. 1510-1515
    • Lai, K.-M.1    Wong, P.C.L.2
  • 26
    • 9344256979 scopus 로고
    • Cell biology
    • (Kenny A. J. and Turner A. J., eds), Elsevier, Amsterdam
    • Luzio J. P., Baron M. D., and Bailyes E. M. (1987) Cell biology, in Mammalian Ectoenzymes (Kenny A. J. and Turner A. J., eds), pp. 111-138. Elsevier, Amsterdam.
    • (1987) Mammalian Ectoenzymes , pp. 111-138
    • Luzio, J.P.1    Baron, M.D.2    Bailyes, E.M.3
  • 29
    • 0024319909 scopus 로고
    • Changes in the activities of adenosine-metabolizing enzymes in six regions of the rat brain on chemical induction of hypothyroidism
    • Mazurkiewicz D. and Saggerson D. (1989) Changes in the activities of adenosine-metabolizing enzymes in six regions of the rat brain on chemical induction of hypothyroidism. Biochem. J. 261, 667-672.
    • (1989) Biochem. J. , vol.261 , pp. 667-672
    • Mazurkiewicz, D.1    Saggerson, D.2
  • 30
    • 0002376293 scopus 로고
    • Adenosine production and metabolism
    • (Stone T. W., ed), Academic Press, London
    • Meghji P. (1991) Adenosine production and metabolism, in Adenosine in the Nervous System (Stone T. W., ed), pp. 25-42. Academic Press, London.
    • (1991) Adenosine in the Nervous System , pp. 25-42
    • Meghji, P.1
  • 31
    • 0020691507 scopus 로고
    • Sedative and electroencephalographic actions of erythro-9-(2-hydroxy-3-nonyl)-adenosine (EHNA): Relationship to inhibition of brain adenosine deaminase
    • Mendelson W. B., Kuravilla A., Watlington T., Goehl K., Paul S. M., and Skolnick P. (1983) Sedative and electroencephalographic actions of erythro-9-(2-hydroxy-3-nonyl)-adenosine (EHNA): relationship to inhibition of brain adenosine deaminase. Psychopharmacology (Berlin) 79, 126-129.
    • (1983) Psychopharmacology (Berlin) , vol.79 , pp. 126-129
    • Mendelson, W.B.1    Kuravilla, A.2    Watlington, T.3    Goehl, K.4    Paul, S.M.5    Skolnick, P.6
  • 32
    • 0025004134 scopus 로고
    • Primary structure of rat liver 5′-nucleotidase deduced from the cDNA. Presence of the COOH-terminal hydrophobic domain for possible post-translational modification by glycophospholipid
    • Misumi Y., Ogata S., Hirose S. and Ikehara Y. (1990) Primary structure of rat liver 5′-nucleotidase deduced from the cDNA. Presence of the COOH-terminal hydrophobic domain for possible post-translational modification by glycophospholipid. J. Biol. Chem. 265, 2178-2183.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2178-2183
    • Misumi, Y.1    Ogata, S.2    Hirose, S.3    Ikehara, Y.4
  • 33
    • 0020397030 scopus 로고
    • Purification and characterization of bovine brain 5′-nucleotidase
    • Montero J. M. and Fes J. B. (1982) Purification and characterization of bovine brain 5′-nucleotidase. J. Neurochem. 39, 982-989.
    • (1982) J. Neurochem. , vol.39 , pp. 982-989
    • Montero, J.M.1    Fes, J.B.2
  • 34
    • 0003116039 scopus 로고
    • Enzymic characteristics and possible role of synaptosomal ecto-adenosine triphosphatase from mammalian brain
    • (Kreutzberg G. W., Reddington M., and Zimmermann H., eds), Springer-Verlag, Berlin
    • Nagy A. (1986) Enzymic characteristics and possible role of synaptosomal ecto-adenosine triphosphatase from mammalian brain, in Cellular Biology of Ectoenzymes (Kreutzberg G. W., Reddington M., and Zimmermann H., eds), pp. 49-59. Springer-Verlag, Berlin.
    • (1986) Cellular Biology of Ectoenzymes , pp. 49-59
    • Nagy, A.1
  • 35
    • 0017076072 scopus 로고
    • The preparation and characterization of synaptic vesicles of high purity
    • Nagy A., Baker R. R., Morris S. J. and Whittaker V. P. (1976) The preparation and characterization of synaptic vesicles of high purity. Brain Res. 109, 285-309.
    • (1976) Brain Res. , vol.109 , pp. 285-309
    • Nagy, A.1    Baker, R.R.2    Morris, S.J.3    Whittaker, V.P.4
  • 36
    • 0019813150 scopus 로고
    • 5′-Nucleotidase from rat heart
    • Naito Y. and Lowenstein J. M. (1981) 5′-Nucleotidase from rat heart. Biochemistry 20, 5188-5194.
    • (1981) Biochemistry , vol.20 , pp. 5188-5194
    • Naito, Y.1    Lowenstein, J.M.2
  • 37
    • 0016610290 scopus 로고
    • The properties and extracellular location of 5′-nucleotidase of the fat-cell plasma membrane
    • Newby A. C., Luzio J. P., and Hales C. N. (1975) The properties and extracellular location of 5′-nucleotidase of the fat-cell plasma membrane. Biochem. J. 146, 625-633.
    • (1975) Biochem. J. , vol.146 , pp. 625-633
    • Newby, A.C.1    Luzio, J.P.2    Hales, C.N.3
  • 38
    • 0026070850 scopus 로고
    • Soluble 5′-nucleotidase activities in rat brain
    • Orford M., Mazurkiewicz D., and Saggerson D. (1991a) Soluble 5′-nucleotidase activities in rat brain. J. Neurochem. 56, 141-146.
    • (1991) J. Neurochem. , vol.56 , pp. 141-146
    • Orford, M.1    Mazurkiewicz, D.2    Saggerson, D.3
  • 39
    • 0025758197 scopus 로고
    • o, in synaptosomal membranes from several regions of the rat brain is increased in hypothyroidism
    • o, in synaptosomal membranes from several regions of the rat brain is increased in hypothyroidism. Biochem. J. 275, 183-186.
    • (1991) Biochem. J. , vol.275 , pp. 183-186
    • Orford, M.1    Mazurkiewicz, D.2    Milligan, G.3    Saggerson, D.4
  • 41
    • 0020669405 scopus 로고
    • Determination of total protein
    • Peterson G. L. (1983) Determination of total protein. Methods Enzymol. 91, 95-119.
    • (1983) Methods Enzymol. , vol.91 , pp. 95-119
    • Peterson, G.L.1
  • 42
    • 0019837565 scopus 로고
    • The role of adenosine and its nucleotides in central synaptic transmission
    • Phillis J. W. and Wu P. H. (1981) The role of adenosine and its nucleotides in central synaptic transmission. Prog. Neurobiol. 16, 187-239.
    • (1981) Prog. Neurobiol. , vol.16 , pp. 187-239
    • Phillis, J.W.1    Wu, P.H.2
  • 43
    • 0026060811 scopus 로고
    • m' 5′-nucleotidase of rat kidney represents solubilized ecto-5′-nucleotidase
    • m' 5′-nucleotidase of rat kidney represents solubilized ecto-5′-nucleotidase. Biochem. J. 273, 409-413.
    • (1991) Biochem. J. , vol.273 , pp. 409-413
    • Piec, G.1    Le Hir, M.2
  • 46
    • 0023154079 scopus 로고
    • ATP release from affinity-purified cholinergic nerve terminals
    • Richardson P. J. and Brown S. J. (1987) ATP release from affinity-purified cholinergic nerve terminals. J. Neurochem. 48, 622-630.
    • (1987) J. Neurochem. , vol.48 , pp. 622-630
    • Richardson, P.J.1    Brown, S.J.2
  • 47
    • 0023661704 scopus 로고
    • Ectoenzymes control adenosine modulation of immunoisolated cholinergic synapses
    • Richardson P. J., Brown S. J., Bailyes E. M., and Luzio J. P. (1987) Ectoenzymes control adenosine modulation of immunoisolated cholinergic synapses. Nature 327, 232-234.
    • (1987) Nature , vol.327 , pp. 232-234
    • Richardson, P.J.1    Brown, S.J.2    Bailyes, E.M.3    Luzio, J.P.4
  • 48
    • 0016683809 scopus 로고
    • Relationship between adenosine concentration and oxygen supply in rat brain
    • Rubio R., Berne R. M., Bockman E. L., and Curnish R. R. (1975) Relationship between adenosine concentration and oxygen supply in rat brain. Am. J. Physiol. 228, 1896-1902.
    • (1975) Am. J. Physiol. , vol.228 , pp. 1896-1902
    • Rubio, R.1    Berne, R.M.2    Bockman, E.L.3    Curnish, R.R.4
  • 49
    • 0023636689 scopus 로고
    • Evidence that adenosine mediates the depression of spinal dorsal horn neurons induced by peripheral vibration in the cat
    • Salter M. W. and Henry J. L. (1987) Evidence that adenosine mediates the depression of spinal dorsal horn neurons induced by peripheral vibration in the cat. Neuroscience 22, 631-650.
    • (1987) Neuroscience , vol.22 , pp. 631-650
    • Salter, M.W.1    Henry, J.L.2
  • 51
    • 0021894314 scopus 로고
    • Adenosine as a neuromodulator
    • Snyder S. H. (1985) Adenosine as a neuromodulator. Annu. Rev. Neurosci. 8, 103-124.
    • (1985) Annu. Rev. Neurosci. , vol.8 , pp. 103-124
    • Snyder, S.H.1
  • 53
    • 0024453115 scopus 로고
    • 5′-Nucleotidases of chicken gizzard and human pancreatic adenocarcinoma cells are anchored to the plasma membrane via a phosphatidylinositol-glycan
    • Stochaj U., Flocke K., Mathes W., and Mannherz H. G. (1989) 5′-Nucleotidases of chicken gizzard and human pancreatic adenocarcinoma cells are anchored to the plasma membrane via a phosphatidylinositol-glycan. Biochem. J. 262, 33-40.
    • (1989) Biochem. J. , vol.262 , pp. 33-40
    • Stochaj, U.1    Flocke, K.2    Mathes, W.3    Mannherz, H.G.4
  • 54
    • 0023227996 scopus 로고
    • Purification of 5′-nucleotidase from human placenta after release from plasma membranes by phosphatidylinositol-specific phospholipase C
    • Thompson L. F., Ruedi J. M., and Low M. G. (1987) Purification of 5′-nucleotidase from human placenta after release from plasma membranes by phosphatidylinositol-specific phospholipase C. Biochem. Biophys. Res. Commun. 145, 118-125.
    • (1987) Biochem. Biophys. Res. Commun. , vol.145 , pp. 118-125
    • Thompson, L.F.1    Ruedi, J.M.2    Low, M.G.3
  • 55
    • 0009482260 scopus 로고
    • Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., and Gordon J. (1979) Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 56
    • 0022976982 scopus 로고
    • Transport and metabolism of 5′-nucleotidase in a rat hepatoma cell line
    • van den Bosch R., Geuze H. J., du Maine A. P. M., and Strous G. J. (1986) Transport and metabolism of 5′-nucleotidase in a rat hepatoma cell line. Eur. J. Biochem. 160, 49-54.
    • (1986) Eur. J. Biochem. , vol.160 , pp. 49-54
    • Van Den Bosch, R.1    Geuze, H.J.2    Du Maine, A.P.M.3    Strous, G.J.4
  • 57
    • 0022979276 scopus 로고
    • Increases in cerebral interstitial fluid adenosine concentration during hypoxia, local potassium infusion, and during ischaemia
    • Van Wylen D. G. L., Park T. S., Rubio R., and Berne R. M. (1986) Increases in cerebral interstitial fluid adenosine concentration during hypoxia, local potassium infusion, and during ischaemia. J. Cereb. Blood Flow Metab. 6, 522-528.
    • (1986) J. Cereb. Blood Flow Metab. , vol.6 , pp. 522-528
    • Van Wylen, D.G.L.1    Park, T.S.2    Rubio, R.3    Berne, R.M.4
  • 58
    • 0010424086 scopus 로고
    • Species specific association of the HNK-1 epitope with 5′-nucleotidase
    • Vogel M., Kowalewski H. J., and Zimmermann H. (1991a) Species specific association of the HNK-1 epitope with 5′-nucleotidase. Biol. Chem. Hoppe Seyler 372, 910-911.
    • (1991) Biol. Chem. Hoppe Seyler , vol.372 , pp. 910-911
    • Vogel, M.1    Kowalewski, H.J.2    Zimmermann, H.3
  • 59
    • 0025781252 scopus 로고
    • Association of the HNK-1 epitope with 5′-nucleotidase from Torpedo marmorata (electric ray) electric organ
    • Vogel M., Kowalewski H. J., Zimmermann H., Janetzko A., Margolis R. U., and Wollny H.-E. (1991b) Association of the HNK-1 epitope with 5′-nucleotidase from Torpedo marmorata (electric ray) electric organ. Biochem. J. 278, 199-202.
    • (1991) Biochem. J. , vol.278 , pp. 199-202
    • Vogel, M.1    Kowalewski, H.J.2    Zimmermann, H.3    Janetzko, A.4    Margolis, R.U.5    Wollny, H.-E.6
  • 60
    • 0026681419 scopus 로고
    • m 5′-nucleotidase from electric rat (Torpedo marmorata) electric organ and bovine cerebral cortex is derived from the glycosyl-phosphatidylinositol-anchored ectoenzyme by phospholipase C cleavage
    • m 5′-nucleotidase from electric rat (Torpedo marmorata) electric organ and bovine cerebral cortex is derived from the glycosyl-phosphatidylinositol-anchored ectoenzyme by phospholipase C cleavage. Biochem. J. 284, 621-624.
    • (1992) Biochem. J. , vol.284 , pp. 621-624
    • Vogel, M.1    Kowalewski, H.2    Zimmermann, H.3    Hooper, N.M.4    Turner, A.J.5
  • 61
    • 0026343113 scopus 로고
    • 5′-Nucleotidase from the electric ray electric lobe; primary structure and relation to mammalian procaryotic enzymes
    • Volknandt W., Vogel M., Pevsner J., Misumi Y., Ikehara Y., and Zimmermann H. (1991) 5′-Nucleotidase from the electric ray electric lobe; primary structure and relation to mammalian procaryotic enzymes. Eur. J. Biochem. 202, 855-861.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 855-861
    • Volknandt, W.1    Vogel, M.2    Pevsner, J.3    Misumi, Y.4    Ikehara, Y.5    Zimmermann, H.6
  • 62
    • 0023018807 scopus 로고
    • Biosynthesis and intracellular transport of rat liver 5′-nucleotidase
    • Wada I., Himeno M., Furuno K., and Kato K. (1986) Biosynthesis and intracellular transport of rat liver 5′-nucleotidase. J. Biol. Chem. 261, 2222-2227.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2222-2227
    • Wada, I.1    Himeno, M.2    Furuno, K.3    Kato, K.4
  • 63
    • 0001827507 scopus 로고
    • Release of adenosine and ATP from nervous tissue
    • (Stone T. W., ed), Academic Press, London
    • White T. D. and Hoehn K. (1991) Release of adenosine and ATP from nervous tissue, in Adenosine in the Nervous System (Stone T. W., ed), pp. 173-195. Academic Press, London.
    • (1991) Adenosine in the Nervous System , pp. 173-195
    • White, T.D.1    Hoehn, K.2
  • 64
    • 0021245914 scopus 로고
    • Adenosine - A selective neuromodulator in the mammalian CNS?
    • Williams M. (1984) Adenosine - a selective neuromodulator in the mammalian CNS? Trends Neurosci. 7, 164-168.
    • (1984) Trends Neurosci. , vol.7 , pp. 164-168
    • Williams, M.1
  • 65
    • 0018945136 scopus 로고
    • Changes in brain bicuculline-induced seizures in rats: Effects of hypoxia and altered systemic blood pressure
    • Winn H. R., Welsh J. E., Rubio R., and Berne R. M. (1980) Changes in brain bicuculline-induced seizures in rats: effects of hypoxia and altered systemic blood pressure. Circ. Res. 47, 568-577.
    • (1980) Circ. Res. , vol.47 , pp. 568-577
    • Winn, H.R.1    Welsh, J.E.2    Rubio, R.3    Berne, R.M.4
  • 66
    • 0020313143 scopus 로고
    • Adenosine measurement by a rapid HPLC-fluorometric method: Induced changes of adenosine content in regions of rat brain
    • Wojcik W. J. and Neff N. H. (1982) Adenosine measurement by a rapid HPLC-fluorometric method: induced changes of adenosine content in regions of rat brain. J. Neurochem. 39, 280-282.
    • (1982) J. Neurochem. , vol.39 , pp. 280-282
    • Wojcik, W.J.1    Neff, N.H.2
  • 67
    • 0023859120 scopus 로고
    • Purification of bovine liver cytosolic 5′-nucleotidase; kinetic and structural studies as compared to the membrane enzyme
    • Zekri M., Harb J., Bernard S., and Meflah K. (1988) Purification of bovine liver cytosolic 5′-nucleotidase; kinetic and structural studies as compared to the membrane enzyme. Eur. J. Biochem. 172, 93-99.
    • (1988) Eur. J. Biochem. , vol.172 , pp. 93-99
    • Zekri, M.1    Harb, J.2    Bernard, S.3    Meflah, K.4
  • 68
    • 0024366392 scopus 로고
    • Differences in the release of 5′-nucleotidase and alkaline phosphatase from plasma membrane of several cell types by PI-PLC
    • Zekri M., Bernard S., Poirier G., Devaux C., and Meflah K. (1989) Differences in the release of 5′-nucleotidase and alkaline phosphatase from plasma membrane of several cell types by PI-PLC. Comp. Biochem. Physiol. [B] 93, 673-679.
    • (1989) Comp. Biochem. Physiol. [B] , vol.93 , pp. 673-679
    • Zekri, M.1    Bernard, S.2    Poirier, G.3    Devaux, C.4    Meflah, K.5
  • 69
    • 0026729643 scopus 로고
    • 5′-Nucleotidase: Molecular structure and functional aspects
    • Zimmermann H. (1992) 5′-Nucleotidase: molecular structure and functional aspects. Biochem. J. 285, 345-365.
    • (1992) Biochem. J. , vol.285 , pp. 345-365
    • Zimmermann, H.1
  • 70
    • 0001782657 scopus 로고
    • Hydrolysis of ATP and formation of adenosine at the surface of cholinergic nerve endings
    • (Kreutzberg G. W., Reddington M., and Zimmermann H., eds), Springer-Verlag, Berlin
    • Zimmermann H., Grondal E. J. M., and Keller F. (1986) Hydrolysis of ATP and formation of adenosine at the surface of cholinergic nerve endings, in Cellular Biology of Ectoenzymes (Kreutzberg G. W., Reddington M., and Zimmermann H., eds), pp. 35-48. Springer-Verlag, Berlin.
    • (1986) Cellular Biology of Ectoenzymes , pp. 35-48
    • Zimmermann, H.1    Grondal, E.J.M.2    Keller, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.