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Volumn 90, Issue 2, 1997, Pages 513-524

Purification and properties of monomeric (G1) forms of acetylcholinesterase secreted by Nippostrongylus brasiliensis

Author keywords

Acetylcholinesterase; Nippostrongylus brasiliensis

Indexed keywords

1,5 BIS(4 ALLYLDIMETHYLAMMONIUMPHENYL)PENTAN 3 ONE DIBROMIDE; ACETYLCHOLINESTERASE; CHOLINESTERASE INHIBITOR; DETERGENT; GALLAMINE; ISO OMPA; MONOMER; PHYSOSTIGMINE; PROPIDIUM IODIDE; SEPHAROSE;

EID: 0031574297     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(97)00202-8     Document Type: Article
Times cited : (26)

References (40)
  • 1
    • 0025764041 scopus 로고
    • The cholinesterases
    • Taylor P The cholinesterases. J Biol Chem. 266:1991;4025-4028.
    • (1991) J Biol Chem , vol.266 , pp. 4025-4028
    • Taylor, P.1
  • 2
    • 0027515387 scopus 로고
    • Structure and functions of acetylcholinesterase and butyrylcholinesterase
    • Massoulié J, Sussman JL, Bon S, Silman I Structure and functions of acetylcholinesterase and butyrylcholinesterase. Prog Brain Res. 98:1993;139-146.
    • (1993) Prog Brain Res , vol.98 , pp. 139-146
    • Massoulié, J.1    Sussman, J.L.2    Bon, S.3    Silman, I.4
  • 3
    • 0023219731 scopus 로고
    • Acetylcholinesterase from bovine caudate nucleus is attached to membranes by a novel subunit distinct from those of acetylcholinesterase in other tissues
    • Inestrosa NC, Roberts WL, Marshall TL, Rosenberry TL Acetylcholinesterase from bovine caudate nucleus is attached to membranes by a novel subunit distinct from those of acetylcholinesterase in other tissues. J Biol Chem. 262:1987;4441-4444.
    • (1987) J Biol Chem , vol.262 , pp. 4441-4444
    • Inestrosa, N.C.1    Roberts, W.L.2    Marshall, T.L.3    Rosenberry, T.L.4
  • 4
    • 0023871065 scopus 로고
    • Modes of attachment of acetylcholinesterase to the surface membrane
    • Silman I, Futerman AH Modes of attachment of acetylcholinesterase to the surface membrane. Eur J Biochem. 170:1987;11-22.
    • (1987) Eur J Biochem , vol.170 , pp. 11-22
    • Silman, I.1    Futerman, A.H.2
  • 5
    • 0023444429 scopus 로고
    • Differences in the glycolipid membrane anchor of bovine and human erythrocyte acetylcholinesterases
    • Roberts WL, Kim BH, Rosenberry TL Differences in the glycolipid membrane anchor of bovine and human erythrocyte acetylcholinesterases. Proc Natl Acad Sci USA. 84:1987;7817-7821.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7817-7821
    • Roberts, W.L.1    Kim, B.H.2    Rosenberry, T.L.3
  • 6
    • 0023721654 scopus 로고
    • Amphiphilic and nonamphiphilic forms of Torpedo cholinesterases: II. Electrophoretic variants and phosphatidylinositol phospholipase C-sensitive and -insensitive forms
    • Bon S, Toutant JP, Méflah K, Massoulié J Amphiphilic and nonamphiphilic forms of Torpedo cholinesterases: II. Electrophoretic variants and phosphatidylinositol phospholipase C-sensitive and -insensitive forms. J Neurochem. 51:1988;786-794.
    • (1988) J Neurochem , vol.51 , pp. 786-794
    • Bon, S.1    Toutant, J.P.2    Méflah, K.3    Massoulié, J.4
  • 7
    • 0020614123 scopus 로고
    • Multiple forms of acetylcholinesterase in the nematode Caenorhabditis elegans
    • Johnson D, Russell RL Multiple forms of acetylcholinesterase in the nematode Caenorhabditis elegans. J Neurochem. 41:1983;30-46.
    • (1983) J Neurochem , vol.41 , pp. 30-46
    • Johnson, D.1    Russell, R.L.2
  • 8
    • 0023845219 scopus 로고
    • Native molecular forms of head acetylcholinesterase from adult Drosophila melanogaster: Quaternary structure and hydrophobic character
    • Toutant J-P, Arpagaus M, Fournier D Native molecular forms of head acetylcholinesterase from adult Drosophila melanogaster: quaternary structure and hydrophobic character. J Neurochem. 50:1988;209-218.
    • (1988) J Neurochem , vol.50 , pp. 209-218
    • Toutant J-P1    Arpagaus, M.2    Fournier, D.3
  • 9
    • 0023885050 scopus 로고
    • Acetylcholinesterase from Musca domestica and Drosophila melanogaster brain are linked to membranes by a glycophospholipid anchor sensitive to an endogenous phospholipase
    • Fournier D, Bergé J-B, Cardoso de Almeida DL, Bordier C Acetylcholinesterase from Musca domestica and Drosophila melanogaster brain are linked to membranes by a glycophospholipid anchor sensitive to an endogenous phospholipase. J Neurochem. 50:1988;1158-1163.
    • (1988) J Neurochem , vol.50 , pp. 1158-1163
    • Fournier, D.1    Bergé J-B2    Cardoso De Almeida, D.L.3    Bordier, C.4
  • 10
    • 0026697345 scopus 로고
    • Acetylcholinesterases of the nematode Steinernema carpocapsae. Characterization of two types of amphiphilic forms differering in their mode of membrane association
    • Arpagaus M, Richier P, Berge J-B, Toutant J-P Acetylcholinesterases of the nematode Steinernema carpocapsae. Characterization of two types of amphiphilic forms differering in their mode of membrane association. Eur J Biochem. 207:1992;1101-1108.
    • (1992) Eur J Biochem , vol.207 , pp. 1101-1108
    • Arpagaus, M.1    Richier, P.2    Berge J-B3    Toutant J-P4
  • 11
    • 0000956804 scopus 로고
    • Neural control of locomotion in Ascaris: anatomy, electrophysiology and biochemistry
    • In: Zuckerman B, editor London: Academic Press
    • Johnson CD, Stretton AOW. Neural control of locomotion in Ascaris: anatomy, electrophysiology and biochemistry. In: Zuckerman B, editor. Nematodes as Biological Models. London: Academic Press, 1980:159-95.
    • (1980) Nematodes As Biological Models , pp. 159-195
    • Johnson, C.D.1    Stretton, A.O.W.2
  • 12
    • 0002452134 scopus 로고
    • The Nervous System
    • In: Wood WB, editor Cold Spring Harbor, NY: Cold Spring Harbor Laboratory
    • Chalfie M, White J. The Nervous System. In: Wood WB, editor. The Nematode Caenorhabditis elegans. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory, 1988:337-91.
    • (1988) The Nematode Caenorhabditis Elegans , pp. 337-391
    • Chalfie, M.1    White, J.2
  • 14
    • 0019525053 scopus 로고
    • A second class of acetylcholinesterase-deficient mutants of the nematode Caenorhabditis elegans
    • Culotti JG, Von Ehrenstein G, Culotti M, Russell RL A second class of acetylcholinesterase-deficient mutants of the nematode Caenorhabditis elegans. Genetics. 97:1981;281-305.
    • (1981) Genetics , vol.97 , pp. 281-305
    • Culotti, J.G.1    Von Ehrenstein, G.2    Culotti, M.3    Russell, R.L.4
  • 15
    • 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 JR, Herman RK, Stern BD, Russell RL The acetylcholinesterase genes of C. elegans: identification of a third gene (ace-3) and mosaic mapping of a synthetic lethal phenotype. Neuron. 1:1988;165-173.
    • (1988) Neuron , vol.1 , pp. 165-173
    • Johnson, C.D.1    Rand, J.R.2    Herman, R.K.3    Stern, B.D.4    Russell, R.L.5
  • 16
    • 0028308367 scopus 로고
    • CDNA sequence, gene structure, and in vitro expression of ace-l, 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 cDNA sequence, gene structure, and in vitro expression of ace-l, the gene encoding acetylcholinesterase of class A in the nematode Caenorhabditis elegans. J Biol Chem. 269:1994;9957-9965.
    • (1994) J Biol Chem , vol.269 , pp. 9957-9965
    • Arpagaus, M.1    Fedon, Y.2    Cousin, X.3    Chatonnet, A.4    Bergé J-B5    Fournier, D.6    Toutant J-P7
  • 17
    • 0015452489 scopus 로고
    • Release of cholinesterase by adult Nippostrongylus brasiliensis in vitro
    • Sanderson BE Release of cholinesterase by adult Nippostrongylus brasiliensis in vitro. Z Parasite. 40:1972;1-7.
    • (1972) Z Parasite , vol.40 , pp. 1-7
    • Sanderson, B.E.1
  • 18
    • 0015907477 scopus 로고
    • Acetylcholinesterase secretion by parasitic nematodes, 1. Evidence for secretion of the enzyme by a number of species
    • Ogilvie BM, Rothwell TLW, Bremner KC, Schitzerling HJ, Nolan J, Keith RK Acetylcholinesterase secretion by parasitic nematodes, 1. Evidence for secretion of the enzyme by a number of species. Int J Parasitol. 3:1973;589-597.
    • (1973) Int J Parasitol , vol.3 , pp. 589-597
    • Ogilvie, B.M.1    Rothwell, T.L.W.2    Bremner, K.C.3    Schitzerling, H.J.4    Nolan, J.5    Keith, R.K.6
  • 19
    • 0019877268 scopus 로고
    • Cholinesterase in the parasitic nematode Stephanurus dentatus. Characterisation and sex dependence of a secretory cholinesterase
    • Rhoads ML Cholinesterase in the parasitic nematode Stephanurus dentatus. Characterisation and sex dependence of a secretory cholinesterase. J Biol Chem. 256:1981;9316-9323.
    • (1981) J Biol Chem , vol.256 , pp. 9316-9323
    • Rhoads, M.L.1
  • 20
    • 0000642174 scopus 로고
    • The fine structure of the excretory system in adult Nippostrongylus brasiliensis (Nematoda) and a suggested function for the enzyme
    • Lee DL The fine structure of the excretory system in adult Nippostrongylus brasiliensis (Nematoda) and a suggested function for the enzyme. Tissue Cell. 2:1970;225-231.
    • (1970) Tissue Cell , vol.2 , pp. 225-231
    • Lee, D.L.1
  • 21
    • 0015962325 scopus 로고
    • The anterior glands of adult Necator americanus (nematode: Strongyloidea)-II. Cytochemical and functional studies
    • McLaren DJ, Burt JS, Ogilvie BM The anterior glands of adult Necator americanus (nematode: Strongyloidea)-II. Cytochemical and functional studies. Int J Parasitol. 4:1974;39-46.
    • (1974) Int J Parasitol , vol.4 , pp. 39-46
    • McLaren, D.J.1    Burt, J.S.2    Ogilvie, B.M.3
  • 22
    • 0025979583 scopus 로고
    • Necator americanus secretory acetylcholinesterase and its purification from excretory-secretory products by affinity chromatography
    • Pritchard DI, Leggett KV, Rogan MT, McKean PG, Brown A Necator americanus secretory acetylcholinesterase and its purification from excretory-secretory products by affinity chromatography. Parasite Immunol. 113:1991;187-199.
    • (1991) Parasite Immunol , vol.113 , pp. 187-199
    • Pritchard, D.I.1    Leggett, K.V.2    Rogan, M.T.3    McKean, P.G.4    Brown, A.5
  • 23
    • 0027952894 scopus 로고
    • The molecular forms of acetylcholinesterase from Necator americanus (Nematoda), a hookworm parasite of the human intestine
    • Pritchard DI, Brown A, Toutant J-P The molecular forms of acetylcholinesterase from Necator americanus (Nematoda), a hookworm parasite of the human intestine. Eur J Biochem. 219:1994;317-323.
    • (1994) Eur J Biochem , vol.219 , pp. 317-323
    • Pritchard, D.I.1    Brown, A.2    Toutant J-P3
  • 24
    • 0028352166 scopus 로고
    • Purification and biochemical characterisation of acetylcholinesterase (ACHE) from the excretory/secretory products of Trichostrongylus colubriformis
    • Griffiths G, Pritchard DI Purification and biochemical characterisation of acetylcholinesterase (ACHE) from the excretory/secretory products of Trichostrongylus colubriformis. Parasitology. 108:1994;579-586.
    • (1994) Parasitology , vol.108 , pp. 579-586
    • Griffiths, G.1    Pritchard, D.I.2
  • 25
    • 0002294584 scopus 로고
    • Secretory cholinesterases of nematodes: Possible functions in the host-parasite relationship
    • Rhoads ML Secretory cholinesterases of nematodes: possible functions in the host-parasite relationship. Trop Vet. 2:1984;3-10.
    • (1984) Trop Vet , vol.2 , pp. 3-10
    • Rhoads, M.L.1
  • 26
    • 0021293734 scopus 로고
    • Acetylcholinesterase secreted by intestinal nematodes: A reinterpretation of its putative role of 'biochemical holdfast'
    • Philipp MT Acetylcholinesterase secreted by intestinal nematodes: a reinterpretation of its putative role of 'biochemical holdfast'. Trans R Soc Trop Med Hyg. 78:1984;138-139.
    • (1984) Trans R Soc Trop Med Hyg , vol.78 , pp. 138-139
    • Philipp, M.T.1
  • 27
    • 0015041059 scopus 로고
    • The effect of host immunity upon some enzymes of the parasitic nematode Nippostrongylus brasiliensis
    • Edwards AJ, Burt JS, Ogilvie BM The effect of host immunity upon some enzymes of the parasitic nematode Nippostrongylus brasiliensis. Parasitology. 62:1971;339-347.
    • (1971) Parasitology , vol.62 , pp. 339-347
    • Edwards, A.J.1    Burt, J.S.2    Ogilvie, B.M.3
  • 28
    • 0015351146 scopus 로고
    • Nippostrongylus brasiliensis: Relation between immune damage and acetylcholinesterase levels
    • Sanderson BE, Jenkins DC, Ogilvie BM Nippostrongylus brasiliensis: relation between immune damage and acetylcholinesterase levels. Int J Parasitol. 2:1972;227-232.
    • (1972) Int J Parasitol , vol.2 , pp. 227-232
    • Sanderson, B.E.1    Jenkins, D.C.2    Ogilvie, B.M.3
  • 29
    • 0017236328 scopus 로고
    • Nippostrongylus brasiliensis: Further studies of the relation between host immunity and worm acetylcholinesterase levels
    • Sanderson BE, Jenkins DC, Phillipson RF Nippostrongylus brasiliensis: further studies of the relation between host immunity and worm acetylcholinesterase levels. Int J Parasitol. 6:1976;99-102.
    • (1976) Int J Parasitol , vol.6 , pp. 99-102
    • Sanderson, B.E.1    Jenkins, D.C.2    Phillipson, R.F.3
  • 30
    • 0026611006 scopus 로고
    • Characterisation of the secretory acetylcholinesterases from adult Nippostrongylus brasiliensis
    • Blackburn CC, Selkirk ME Characterisation of the secretory acetylcholinesterases from adult Nippostrongylus brasiliensis. Mol Biochem Parasitol. 53:1992;79-88.
    • (1992) Mol Biochem Parasitol , vol.53 , pp. 79-88
    • Blackburn, C.C.1    Selkirk, M.E.2
  • 31
    • 0026483952 scopus 로고
    • Amphiphilic forms of butyrylcholinesterase in mucosal cells of rat intestine
    • Sine J-P, Toutant J-P, Weigel P, Colas B Amphiphilic forms of butyrylcholinesterase in mucosal cells of rat intestine. Biochemistry. 31:1992;10893-10900.
    • (1992) Biochemistry , vol.31 , pp. 10893-10900
    • Sine J-P1    Toutant J-P2    Weigel, P.3    Colas, B.4
  • 33
    • 78651153462 scopus 로고
    • A 'direct-coloring' method for cholinesterases
    • Karnovsky MJ, Roots L A 'direct-coloring' method for cholinesterases. J Histochem Cytochem. 12:1964;219-221.
    • (1964) J Histochem Cytochem , vol.12 , pp. 219-221
    • Karnovsky, M.J.1    Roots, L.2
  • 35
    • 0001537321 scopus 로고
    • Two selective inhibitors of cholinesterase
    • Austin L, Berry WK Two selective inhibitors of cholinesterase. Biochem J. 54:1953;695-700.
    • (1953) Biochem J , vol.54 , pp. 695-700
    • Austin, L.1    Berry, W.K.2
  • 36
    • 0025871854 scopus 로고
    • Characterization of proteolytic enzymes from larval and adult Nippostrongylus brasiliensis
    • Healer J, Ashall F, Maizels RM Characterization of proteolytic enzymes from larval and adult Nippostrongylus brasiliensis. Parasitology. 103:1991;305-314.
    • (1991) Parasitology , vol.103 , pp. 305-314
    • Healer, J.1    Ashall, F.2    Maizels, R.M.3
  • 37
    • 0026031111 scopus 로고
    • Role of the peripheral anionic site on acetylcholinesterase: Inhibition by substrates and coumarin derivatives
    • Radic Z, Reiner E, Taylor P Role of the peripheral anionic site on acetylcholinesterase: inhibition by substrates and coumarin derivatives. Mol Pharmacol. 39:1991;98-104.
    • (1991) Mol Pharmacol , vol.39 , pp. 98-104
    • Radic, Z.1    Reiner, E.2    Taylor, P.3
  • 38
    • 0027517144 scopus 로고
    • Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- And butyryl-cholinesterase inhibitors
    • Radic Z, Pickering NA, Vellom DC, Camp S, Taylor P Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyryl-cholinesterase inhibitors. Biochemistry. 32:1993;12074-12084.
    • (1993) Biochemistry , vol.32 , pp. 12074-12084
    • Radic, Z.1    Pickering, N.A.2    Vellom, D.C.3    Camp, S.4    Taylor, P.5
  • 39
    • 0028177161 scopus 로고
    • Differential effects of 'peripheral' site ligands on Torpedo and chicken acetylcholinesterase
    • Eichler J, Anselmet A, Sussman JL, Massoulié J, Silman I Differential effects of 'peripheral' site ligands on Torpedo and chicken acetylcholinesterase. Mol Pharmacol. 45:1994;335-340.
    • (1994) Mol Pharmacol , vol.45 , pp. 335-340
    • Eichler, J.1    Anselmet, A.2    Sussman, J.L.3    Massoulié, J.4    Silman, I.5
  • 40
    • 0026794595 scopus 로고
    • Expression of recombinant acetylcholinesterase in a baculovirus system: Kinetic properties of glutamate 199 mutants
    • Radic Z, Gibney G, Kawamoto S, MacPhee-Quigley K, Bongiorno C, Taylor P Expression of recombinant acetylcholinesterase in a baculovirus system: kinetic properties of glutamate 199 mutants. Biochemistry. 31:1992;9760-9767.
    • (1992) Biochemistry , vol.31 , pp. 9760-9767
    • Radic, Z.1    Gibney, G.2    Kawamoto, S.3    MacPhee-Quigley, K.4    Bongiorno, C.5    Taylor, P.6


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