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Volumn 79, Issue 7, 1997, Pages 397-405

Acetylcholinesterase in Spirographis spallanzanii (Polychaeta: Sedentaria): Presence of two dimeric membrane-bound forms

Author keywords

Annelid polychaete; Cell membrane anchoring; Cholinesterase; Molecular forms; Phosphatidylinositol

Indexed keywords

ACETYLCHOLINESTERASE; EDROPHONIUM; MEMBRANE ENZYME; PHYSOSTIGMINE; PROCAINAMIDE; TRITON X 100;

EID: 0030732474     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(97)86149-4     Document Type: Article
Times cited : (6)

References (40)
  • 3
    • 0020021171 scopus 로고
    • The molecular forms of cholinesterase in vertebrates
    • Massoulié J, Bon S (1982) The molecular forms of cholinesterase in vertebrates. Annu Rev Neurosci 5, 57-106
    • (1982) Annu Rev Neurosci , vol.5 , pp. 57-106
    • Massoulié, J.1    Bon, S.2
  • 4
    • 0023871065 scopus 로고
    • Modes of attachment of acetylcholinesterase to the surface membrane
    • Silman I, Futerman A H (1987) Modes of attachment of acetylcholinesterase to the surface membrane. Eur J Biochem 170, 11-22
    • (1987) Eur J Biochem , vol.170 , pp. 11-22
    • Silman, I.1    Futerman, A.H.2
  • 7
    • 0023665033 scopus 로고
    • Isolation and characterization of acetylcholinesterase from Drosophila
    • Gnagey AL, Forte M, Rosenberry TL (1987) Isolation and characterization of acetylcholinesterase from Drosophila. J Biol Chem 262, 13290-13298
    • (1987) J Biol Chem , vol.262 , pp. 13290-13298
    • Gnagey, A.L.1    Forte, M.2    Rosenberry, T.L.3
  • 8
    • 0024489712 scopus 로고
    • Insect acetylcholinesterase: Catalytic properties, tissue distribution and molecular forms
    • Toutant J-P (1989) Insect acetylcholinesterase: catalytic properties, tissue distribution and molecular forms. Prog Neurobiol 32, 423-446
    • (1989) Prog Neurobiol , vol.32 , pp. 423-446
    • Toutant, J.-P.1
  • 9
    • 0027951250 scopus 로고
    • Presence of a soluble tetrameric (blood) and membrane-bound dimeric forms of cholinesterase in the mollusk Murex brandaris (Gastropoda: Neogastropoda)
    • Talesa V, Principato GB, Giovannini E, Norton SJ, Rosi G (1994) Presence of a soluble tetrameric (blood) and membrane-bound dimeric forms of cholinesterase in the mollusk Murex brandaris (Gastropoda: Neogastropoda). J Exp Zool 270, 233-244
    • (1994) J Exp Zool , vol.270 , pp. 233-244
    • Talesa, V.1    Principato, G.B.2    Giovannini, E.3    Norton, S.J.4    Rosi, G.5
  • 10
    • 0028980217 scopus 로고
    • Acetylcholinesterase in tentacles of Octopus vulgaris (Cephalopoda). Histochemical localization and characterization of a specific high salt-soluble and heparin-soluble fraction of globular forms
    • Talesa V, Grauso M, Giovannini E, Rosi G, Toutant J-P (1995) Acetylcholinesterase in tentacles of Octopus vulgaris (Cephalopoda). Histochemical localization and characterization of a specific high salt-soluble and heparin-soluble fraction of globular forms. Neurochem Int 27, 201-211
    • (1995) Neurochem Int , vol.27 , pp. 201-211
    • Talesa, V.1    Grauso, M.2    Giovannini, E.3    Rosi, G.4    Toutant, J.-P.5
  • 11
    • 0028959657 scopus 로고
    • Solubilization, molecular forms, purification and substrate specificity of two acetylcholinesterases in the medicinal leech (Hirudo medicinalis)
    • Talesa V, Grauso M, Giovannini E, Rosi G, Toutant J-P (1995) Solubilization, molecular forms, purification and substrate specificity of two acetylcholinesterases in the medicinal leech (Hirudo medicinalis). Biochem J 306, 687-692
    • (1995) Biochem J , vol.306 , pp. 687-692
    • Talesa, V.1    Grauso, M.2    Giovannini, E.3    Rosi, G.4    Toutant, J.-P.5
  • 12
    • 0029953632 scopus 로고    scopus 로고
    • Acetylcholinesterase in Dendrobaena veneta (Oligochaeta: Opisthopora) is present with forms sensitive and insensitive to phosphatidylinositol phospholipase C. Biochemical characterization and histochemical localization in the nervous system
    • TalesaV, Romani R, Rosi G, Giovannini E (1996) Acetylcholinesterase in Dendrobaena veneta (Oligochaeta: Opisthopora) is present with forms sensitive and insensitive to phosphatidylinositol phospholipase C. Biochemical characterization and histochemical localization in the nervous system. Eur J Biochem 238, 538-548
    • (1996) Eur J Biochem , vol.238 , pp. 538-548
    • Talesa, V.1    Romani, R.2    Rosi, G.3    Giovannini, E.4
  • 13
    • 0023985973 scopus 로고
    • The acetylcholinesterase genes of C elegans: Identification of a third gene (ace-3) and mosaic mapping of a synthetic lethal phenotype
    • Johnson CD, Rand JB, Herman RK, Stern BD, Russel RL (1988) The acetylcholinesterase genes of C elegans: identification of a third gene (ace-3) and mosaic mapping of a synthetic lethal phenotype. Neuron 1, 165-173
    • (1988) Neuron , vol.1 , pp. 165-173
    • Johnson, C.D.1    Rand, J.B.2    Herman, R.K.3    Stern, B.D.4    Russel, R.L.5
  • 14
    • 0028308367 scopus 로고
    • cDNA sequence, gene structure and in vitro expression of ace-1, the gene encoding acetylcholinesterase of class A in the nematode Caenorhabditis elegans
    • Arpagaus M, Fedon Y, Cousin X, Chatonnet A, Bergé J-B, Fournier D, Toutant J-P (1994) cDNA sequence, gene structure and in vitro expression of ace-1, the gene encoding acetylcholinesterase of class A in the nematode Caenorhabditis elegans. J Biol Chem 269, 1101-1108
    • (1994) J Biol Chem , vol.269 , pp. 1101-1108
    • Arpagaus, M.1    Fedon, Y.2    Cousin, X.3    Chatonnet, A.4    Bergé, J.-B.5    Fournier, D.6    Toutant, J.-P.7
  • 15
    • 0343170552 scopus 로고
    • Pharmacology of cholinergic system in annelids
    • Michelson MJ, ed, Pergamon Press, Oxford
    • Rozhkova EK (1973) Pharmacology of cholinergic system in annelids. In: International encyclopedia of pharmacology and therapeutics 85/1 (Michelson MJ, ed), Pergamon Press, Oxford, 241-344
    • (1973) International Encyclopedia of Pharmacology and Therapeutics , vol.85 , Issue.1 , pp. 241-344
    • Rozhkova, E.K.1
  • 16
    • 0015551118 scopus 로고
    • Chemical transmission in invertebrate central nervous system and neuromuscular junction
    • Gerschenfeld HM (1973) Chemical transmission in invertebrate central nervous system and neuromuscular junction. Physiol Rev 53, 1-119
    • (1973) Physiol Rev , vol.53 , pp. 1-119
    • Gerschenfeld, H.M.1
  • 17
    • 0002640869 scopus 로고
    • Phylogeny of the cholinergic synapse
    • (Whittaker VP, ed) Springer-Verlag, Berlin, Heidelberg
    • Wächtler K (1988) Phylogeny of the cholinergic synapse. In: The cholinergic synapse (Whittaker VP, ed) Springer-Verlag, Berlin, Heidelberg, 57-80
    • (1988) The Cholinergic Synapse , pp. 57-80
    • Wächtler, K.1
  • 20
    • 0020825373 scopus 로고
    • Isolation of the secretory form of soluble acetylcholinesterase by using affinity chromatography on edrophonium-sepharose
    • Hodgson AJ, Chubb IW (1983) Isolation of the secretory form of soluble acetylcholinesterase by using affinity chromatography on edrophonium-Sepharose. J Neurochem 41, 654-662
    • (1983) J Neurochem , vol.41 , pp. 654-662
    • Hodgson, A.J.1    Chubb, I.W.2
  • 21
    • 0020581758 scopus 로고
    • Use of procainamide gels in the purification of human and horse serum cholinesterases
    • Ralston SJ, Main AR, Kilpatrick BF, Chasson AL (1983) Use of procainamide gels in the purification of human and horse serum cholinesterases. Biochem 7211, 243-250
    • (1983) Biochem J , vol.211 , pp. 243-250
    • Ralston, S.J.1    Main, A.R.2    Kilpatrick, B.F.3    Chasson, A.L.4
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 0030481897 scopus 로고    scopus 로고
    • Presence of an acetylcholinesterase in the cnidarian Actinia equina (Anthozoa: Actiniaria) and of a thiocholine ester-hydrolyzing esterase in the sponge Spongia officinalis (Demospongiae: Keratosa)
    • Talesa V, Romani R, Rosi G, Giovannini E (1996) Presence of an acetylcholinesterase in the cnidarian Actinia equina (Anthozoa: Actiniaria) and of a thiocholine ester-hydrolyzing esterase in the sponge Spongia officinalis (Demospongiae: Keratosa). J Exp Zool 276, 102-111
    • (1996) J Exp Zool , vol.276 , pp. 102-111
    • Talesa, V.1    Romani, R.2    Rosi, G.3    Giovannini, E.4
  • 27
    • 0000954548 scopus 로고
    • Vertebrate cholinesterases: Structure and types of interaction
    • Massoulié J, Toutant J-P (1988) Vertebrate cholinesterases: structure and types of interaction. Handb Exp Pharmacol 86, 167-224
    • (1988) Handb Exp Pharmacol , vol.86 , pp. 167-224
    • Massoulié, J.1    Toutant, J.-P.2
  • 30
    • 39749187675 scopus 로고
    • A theory of gel filtration and its experimental verification
    • Laurent TC, Killander J (1964) A theory of gel filtration and its experimental verification. J Chromatogr 14, 317-330
    • (1964) J Chromatogr , vol.14 , pp. 317-330
    • Laurent, T.C.1    Killander, J.2
  • 32
    • 0027377697 scopus 로고
    • Evidence for a molecular polymorphism of Cholinesterase in Sepia officinalis (Cephalopoda, Decapoda)
    • Talesa V, Principato GB, Giovannini E, Grauso M, Rosi G (1993) Evidence for a molecular polymorphism of Cholinesterase in Sepia officinalis (Cephalopoda, Decapoda). Comp Biochem Physiol 106B, 557-562
    • (1993) Comp Biochem Physiol , vol.106 B , pp. 557-562
    • Talesa, V.1    Principato, G.B.2    Giovannini, E.3    Grauso, M.4    Rosi, G.5
  • 33
    • 0021338810 scopus 로고
    • Structure of human erythrocyte acetylcholinesterase. Characterization of inter-subunit disulfide bonding and detergent interaction
    • Rosenberry TL, Scoggin DM (1984) Structure of human erythrocyte acetylcholinesterase. Characterization of inter-subunit disulfide bonding and detergent interaction. J Biol Chem 259, 5643-5652
    • (1984) J Biol Chem , vol.259 , pp. 5643-5652
    • Rosenberry, T.L.1    Scoggin, D.M.2
  • 34
    • 0023721654 scopus 로고
    • Amphiphilic and nonamphiphilic forms of Torpedo cholinesterases: II. Electrophoretic variants and phosphatidylinositol phospholipase c-sensitive and -insensitive forms
    • Bon S, Toutant J-P, Méflah K, Massoulié J (1988) Amphiphilic and nonamphiphilic forms of Torpedo cholinesterases: II. Electrophoretic variants and phosphatidylinositol phospholipase C-sensitive and -insensitive forms. J Neurochem 51, 786-794
    • (1988) J Neurochem , vol.51 , pp. 786-794
    • Bon, S.1    Toutant, J.-P.2    Méflah, K.3    Massoulié, J.4
  • 35
    • 0001428370 scopus 로고
    • Molecular mechanisms for hydrolytic enzyme action. I, II, III, IV. Structure of the active center and the reaction mechanism
    • Krupka RM, Laidler KJ (1961) Molecular mechanisms for hydrolytic enzyme action. I, II, III, IV. Structure of the active center and the reaction mechanism. J Am Chem Soc 83, 1445-1460
    • (1961) J Am Chem Soc , vol.83 , pp. 1445-1460
    • Krupka, R.M.1    Laidler, K.J.2
  • 36
    • 0015290174 scopus 로고
    • Purification and properties of brain acetylcholinesterase (EC 3.1.1.7)
    • Chan SL, Sirachi DY, Trevor AJ (1972) Purification and properties of brain acetylcholinesterase (EC 3.1.1.7). J Neurochem 19, 437-447
    • (1972) J Neurochem , vol.19 , pp. 437-447
    • Chan, S.L.1    Sirachi, D.Y.2    Trevor, A.J.3
  • 39
    • 0016593463 scopus 로고
    • Acetylcholinesterase
    • Rosenberry TL (1975) Acetylcholinesterase. Adv Enzymol 43, 103-218
    • (1975) Adv Enzymol , vol.43 , pp. 103-218
    • Rosenberry, T.L.1


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