메뉴 건너뛰기




Volumn 53, Issue 5-6, 1998, Pages 407-415

Choline Acetyltransferase from the Electric Organ of Electrophorus electricus (L.)-Physicochemical Characterization and Immunochemical Identification

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL COENZYME A H 3; AMMONIUM SULFATE; BUFFER; CENTRIFUGATION; CHOLINE ACETYLTRANSFERASE; COLUMN CHROMATOGRAPHY; DROSOPHILA MELANOGASTER; ELECTRIC ORGAN; ELECTROPHORUS; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME REGULATION; GEL FILTRATION; IMMUNOANALYSIS; MOLECULAR WEIGHT; PRECIPITATION; SDS POLYACRYLAMIDE GEL ELECTROPHORESIS; SODIUM DIHYDROGEN PHOSPHATE; SOLUBILIZATION; WESTERN BLOTTING;

EID: 2642616235     PISSN: 09395075     EISSN: None     Source Type: Journal    
DOI: 10.1515/znc-1998-5-617     Document Type: Article
Times cited : (6)

References (40)
  • 1
    • 0022601116 scopus 로고
    • The effects of physiostigmine and scopolamine on recognition memory in monkeys
    • Aigner T. G. and Mishkin M. (1986). The effects of physiostigmine and scopolamine on recognition memory in monkeys. Behav. Neural. Biol. 45, 81-87.
    • (1986) Behav. Neural. Biol. , vol.45 , pp. 81-87
    • Aigner, T.G.1    Mishkin, M.2
  • 2
    • 0019972810 scopus 로고
    • Cholinergic hypothesis of geriatric memory dysfunction
    • Bartus R. T., Dean R. D., Beer B. and Lippa A. S. (1982). Cholinergic hypothesis of geriatric memory dysfunction. Science 217, 408-414.
    • (1982) Science , vol.217 , pp. 408-414
    • Bartus, R.T.1    Dean, R.D.2    Beer, B.3    Lippa, A.S.4
  • 3
    • 0022363496 scopus 로고
    • Immu noaffinity purification of choline acetyltransferase: Comparison of the brain and placental enzymes
    • Bruce G., Wainer B. H. and Hersh L. B. (1985), Immu noaffinity purification of choline acetyltransferase: Comparison of the brain and placental enzymes. J. Neurochem. 45, 611-620.
    • (1985) J. Neurochem. , vol.45 , pp. 611-620
    • Bruce, G.1    Wainer, B.H.2    Hersh, L.B.3
  • 4
    • 0042837104 scopus 로고
    • Desmin expression in the electric organs of Electrophorus electricus (L.)
    • Costa M. L., Mermelstein C. S., Moura Neto V. and Chagas C. (1988). Desmin expression in the electric organs of Electrophorus electricus (L.). J. Cell Biochem. Supp. 12c. 323.
    • (1988) J. Cell Biochem. , pp. 323
    • Costa, M.L.1    Mermelstein, C.S.2    Moura Neto, V.3    Chagas, C.4
  • 5
    • 0004286331 scopus 로고
    • Characterisation de la desinine dans l'organe électrique de I'Electrophorus electricus (L.)
    • série III
    • Costa M. L., Oliveira M. M., Alberti Jr., O., Moura Neto V. and Chagas C. (1986), Characterisation de la desinine dans l'organe électrique de I'Electrophorus electricus (L.). C. R. Acad. Sci. Paris 303, série III, 547-550.
    • (1986) C. R. Acad. Sci. Paris , vol.303 , pp. 547-550
    • Costa, M.L.1    Oliveira, M.M.2    Alberti, O.3    Moura Neto, V.4    Chagas, C.5
  • 6
    • 0022466343 scopus 로고
    • Amphiphilic and hydrophilic forms of choline-O-acetyltransferase in cholinergic nerve endings of Torpedo
    • Eder-Colli L., Amato S. and Froment Y. (1986), Amphiphilic and hydrophilic forms of choline-O-acetyltransferase in cholinergic nerve endings of Torpedo. Neuroscience 19, 275-287.
    • (1986) Neuroscience , vol.19 , pp. 275-287
    • Eder-Colli, L.1    Amato, S.2    Froment, Y.3
  • 7
    • 0016468979 scopus 로고
    • Rapid radiochemical method for the determination of choline acetyltransferase
    • Fonnun F. A. (1975). Rapid radiochemical method for the determination of choline acetyltransferase. J. Neurochem. 24, 407-409.
    • (1975) J. Neurochem. , vol.24 , pp. 407-409
    • Fonnun, F.A.1
  • 8
    • 2642646192 scopus 로고
    • TLC identification of Ach after biosynthesis with the electric organ
    • Hasson-Voloch A. and Simas D. (1969), TLC identification of Ach after biosynthesis with the electric organ. Anais da Acad. Brasil, de Ciências 41, 235-237.
    • (1969) Anais da Acad. Brasil, de Ciências , vol.41 , pp. 235-237
    • Hasson-Voloch, A.1    Simas, D.2
  • 9
    • 0020667155 scopus 로고
    • Creatine kinase from the electric organ of Electrophorus electricus (L.) - Isozyme analysis
    • Hazan-Carneiro L. V. and Hassón-Voloch A. (1983), Creatine kinase from the electric organ of Electrophorus electricus (L.) - Isozyme analysis. Int. Biochem. 15. 111-114.
    • (1983) Int. Biochem. , vol.15 , pp. 111-114
    • Hazan-Carneiro, L.V.1    Hassón-Voloch, A.2
  • 10
    • 0028273219 scopus 로고
    • Choline acetyltransferase: Celebrating its fiftieth year
    • Hersh L. B. and Wu D. (1994), Choline acetyltransferase: Celebrating its fiftieth year. J. Neurochem. 62, 1653-1663.
    • (1994) J. Neurochem. , vol.62 , pp. 1653-1663
    • Hersh, L.B.1    Wu, D.2
  • 11
    • 0029150271 scopus 로고
    • Activation of choline acetyltransferase by limited proteolysis
    • Hersh L. B. and Wu D. (1995), Activation of choline acetyltransferase by limited proteolysis. J. Biol. Chem. 270, 19395-19401.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19395-19401
    • Hersh, L.B.1    Wu, D.2
  • 12
    • 0024499097 scopus 로고
    • Choline acetyltransferase activities in single spinal motor neurons from patients with Amyotrophic Lateral Sclerosis
    • Kato T. (1989), Choline acetyltransferase activities in single spinal motor neurons from patients with Amyotrophic Lateral Sclerosis. J. Neurochem. 52, 636-640.
    • (1989) J. Neurochem. , vol.52 , pp. 636-640
    • Kato, T.1
  • 13
    • 84919876011 scopus 로고
    • Membrane potentials in the electroplates of the electric eel
    • Keynes R. D. and Martins-Ferreira H. (1953), Membrane potentials in the electroplates of the electric eel. J. Physiology 119, 315-351.
    • (1953) J. Physiology , vol.119 , pp. 315-351
    • Keynes, R.D.1    Martins-Ferreira, H.2
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of head of bacteriophage T4
    • Laemmli U. K. (1970), Cleavage of structural proteins during the assembly of head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 10444252700 scopus 로고
    • Über humorale Übertragbarkeit der Hirnentwicklung
    • Loewi O. (1921), Über humorale Übertragbarkeit der Hirnentwicklung. Pflügers Arch. 189, 239-242.
    • (1921) Pflügers Arch. , vol.189 , pp. 239-242
    • Loewi, O.1
  • 17
    • 0015311923 scopus 로고
    • Multiple forms of choline acetyltransferase in several species demonstrated by isoelectric focusing
    • Malthe-Sorenssen and Fonnun F. (1972). Multiple forms of choline acetyltransferase in several species demonstrated by isoelectric focusing. Biochem. J. 127, 229-236.
    • (1972) Biochem. J. , vol.127 , pp. 229-236
    • Malthe-Sorenssen1    Fonnun, F.2
  • 18
    • 0024207424 scopus 로고
    • Choline acetyltransferase-like activity bound to neuronal plasma membranes
    • Massarelli R., Ferret B., Sorrentino G., Hatton H. and Kanfer J. N. (1988), Choline acetyltransferase-like activity bound to neuronal plasma membranes. Neurochem. Res. 13, 1193-1198.
    • (1988) Neurochem. Res. , vol.13 , pp. 1193-1198
    • Massarelli, R.1    Ferret, B.2    Sorrentino, G.3    Hatton, H.4    Kanfer, J.N.5
  • 19
    • 0017555378 scopus 로고
    • Choline acetyltransferase
    • Mautner H. G. (1977), Choline acetyltransferase. CRC Crit. Rev. Biochem. 4, 341-370.
    • (1977) CRC Crit. Rev. Biochem. , vol.4 , pp. 341-370
    • Mautner, H.G.1
  • 20
    • 0000201092 scopus 로고
    • Choline acetyltransferase
    • (Boulton A. A., Baker G. B. and Yu P. H. ed). Humana Press, Clifton, New Jersey
    • Mautner, H. G. (1986) - Choline acetyltransferase. In: Neurotransmitter Enzymes, vol. 5 (Boulton A. A., Baker G. B. and Yu P. H. ed). Humana Press, Clifton, New Jersey, pp 273-317.
    • (1986) Neurotransmitter Enzymes , vol.5 , pp. 273-317
    • Mautner, H.G.1
  • 21
    • 0026644564 scopus 로고
    • Synthesis and release of acetylcholine in the rabbit kidney cortex
    • Meyer E. M. (1992), Synthesis and release of acetylcholine in the rabbit kidney cortex. Life sci. 51, 1699-1703.
    • (1992) Life sci. , vol.51 , pp. 1699-1703
    • Meyer, E.M.1
  • 22
    • 0013817044 scopus 로고
    • Species differences in subcellular distribution of choline acetylase in the CNS
    • McCaman R. E., Rodriguez De Lores Arnaiz G. and De Robertis E. (1965), Species differences in subcellular distribution of choline acetylase in the CNS. J. Neurochem. 12, 927-935.
    • (1965) J. Neurochem. , vol.12 , pp. 927-935
    • McCaman, R.E.1    Rodriguez De Lores Arnaiz, G.2    De Robertis, E.3
  • 23
    • 0022142941 scopus 로고
    • Astrocytic-cerebellar cell clones synthesize the isoforms of the tubulin protein family
    • Moura Neto V., Mallat M., Alliot F., Pessac B. and Prochiantz A. (1985), Astrocytic-cerebellar cell clones synthesize the isoforms of the tubulin protein family. Neuroscience, 16, 333-341.
    • (1985) Neuroscience , vol.16 , pp. 333-341
    • Moura Neto, V.1    Mallat, M.2    Alliot, F.3    Pessac, B.4    Prochiantz, A.5
  • 24
    • 0019807067 scopus 로고
    • Choline acetyltransferase in skeletal muscle from patients with Myasthenia Gravis
    • Molenaar P. C., Newsom-Davis J., Polak L. and Vicent A. (1981), Choline acetyltransferase in skeletal muscle from patients with Myasthenia Gravis. J. Neurochem. 37, 1081-1088.
    • (1981) J. Neurochem. , vol.37 , pp. 1081-1088
    • Molenaar, P.C.1    Newsom-Davis, J.2    Polak, L.3    Vicent, A.4
  • 25
    • 0000579645 scopus 로고
    • The formation of acetylcholine. A new enzyme choline acetylase
    • Nachmansohn D. and Machado A. L. (1943), The formation of acetylcholine. A new enzyme choline acetylase. J. Neurophysiol. 6, 397-403.
    • (1943) J. Neurophysiol. , vol.6 , pp. 397-403
    • Nachmansohn, D.1    Machado, A.L.2
  • 26
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrel P. H. (1975), High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250, 4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrel, P.H.1
  • 27
    • 0017174765 scopus 로고
    • Preparation and characterization of two isozymes of choline acetyltransferase from squid head ganglia. Self-association, molecular weight determinations and studies with inactivating antisera
    • Polsky R. and Shuster L. (1976). Preparation and characterization of two isozymes of choline acetyltransferase from squid head ganglia. Self-association, molecular weight determinations and studies with inactivating antisera. Biochem. and Biophys. Acta 445, 43-66.
    • (1976) Biochem. and Biophys. Acta , vol.445 , pp. 43-66
    • Polsky, R.1    Shuster, L.2
  • 28
    • 0014429880 scopus 로고
    • Choline acetyltransferase from rat brain
    • Potter L. T., Glover V. A. S. and Saelens J. K. (1968), Choline acetyltransferase from rat brain. J. Biol. Chem. 243, 3864-3870.
    • (1968) J. Biol. Chem. , vol.243 , pp. 3864-3870
    • Potter, L.T.1    Glover, V.A.S.2    Saelens, J.K.3
  • 29
    • 0017625686 scopus 로고
    • Choline Acetyltransferase: A review with special reference to its cellular and subcellular localization
    • Rossier J. (1977), Choline Acetyltransferase: A review with special reference to its cellular and subcellular localization. Int. Rev. Neurobiol. 20, 284-337.
    • (1977) Int. Rev. Neurobiol. , vol.20 , pp. 284-337
    • Rossier, J.1
  • 30
    • 0015631967 scopus 로고
    • Improved purification of rat brain choline acetyltransferase by using an immunoabsorbent
    • Rossier J., Bauman A. and Benda P. (1973), Improved purification of rat brain choline acetyltransferase by using an immunoabsorbent. FEBS Lett. 32, 231-234.
    • (1973) FEBS Lett. , vol.32 , pp. 231-234
    • Rossier, J.1    Bauman, A.2    Benda, P.3
  • 31
    • 0020478788 scopus 로고
    • Purification of choline acetyltransferase from Drosophila melanogaster
    • Salvaterra P. M., Slemmon J. R., Crawford G. D. and Roberts E. (1982), Purification of choline acetyltransferase from Drosophila melanogaster. J. Biol. Chem. 257, 3847-3852.
    • (1982) J. Biol. Chem. , vol.257 , pp. 3847-3852
    • Salvaterra, P.M.1    Slemmon, J.R.2    Crawford, G.D.3    Roberts, E.4
  • 32
    • 0027270596 scopus 로고
    • Basal synthesis of acetylcholine in hippocampal synaptossomes is not dependent upon membrane-bound choline acetyltransferase activity
    • Schmidt B. M. and Rylett R. J. (1993), Basal synthesis of acetylcholine in hippocampal synaptossomes is not dependent upon membrane-bound choline acetyltransferase activity. Neuroscience 54, 649-656.
    • (1993) Neuroscience , vol.54 , pp. 649-656
    • Schmidt, B.M.1    Rylett, R.J.2
  • 33
    • 0018833731 scopus 로고
    • A comparison of solubilized and membrane bound forms of choline-O- acetyltransferase (E. C. 2.3.1.6) in mouse brain nerve endings
    • Smith C. P. and Carroll P. T. (1980), A comparison of solubilized and membrane bound forms of choline-O- acetyltransferase (E. C. 2.3.1.6) in mouse brain nerve endings. Brain Res. 185, 363-371.
    • (1980) Brain Res. , vol.185 , pp. 363-371
    • Smith, C.P.1    Carroll, P.T.2
  • 34
    • 2642611059 scopus 로고
    • 2+on the cholineacetyltransf- erase activity of Electrophorus electricus (L.) electric organ
    • 2+on the cholineacetyltransf- erase activity of Electrophorus electricus (L.) electric organ. An. Acad. Brasil. Ciênc. 44, 263-271.
    • (1972) An. Acad. Brasil. Ciênc. , vol.44 , pp. 263-271
    • Soares, M.N.A.1    Hassón-Voloch, A.2
  • 35
    • 0017662913 scopus 로고
    • Biochemical and cytochemical localisation of ATPases on the membranes of the electrocyte of Electrophorus electricus (L.)
    • Somló, C., Souza W., Machado R. D. and Hasson-Voloch A. (1977), Biochemical and cytochemical localisation of ATPases on the membranes of the electrocyte of Electrophorus electricus (L.). Cell Tiss. Res. 185, 115-128.
    • (1977) Cell Tiss. Res. , vol.185 , pp. 115-128
    • Somló, C.1    Souza, W.2    Machado, R.D.3    Hasson-Voloch, A.4
  • 36
    • 0029092794 scopus 로고
    • The human choline acetyltransferase gene encodes two proteins
    • Strauss W. L., Grosman D. D., Lorenzi M. V. and Trindad A. C. (1995), The human choline acetyltransferase gene encodes two proteins. J. Neurochem. 65, 484-491.
    • (1995) J. Neurochem. , vol.65 , pp. 484-491
    • Strauss, W.L.1    Grosman, D.D.2    Lorenzi, M.V.3    Trindad, A.C.4
  • 37
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staeheli T. I. and Gordon J. (1979), Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natn. Acad. Sci. USA. 76, 4350-4354.
    • (1979) Proc. Natn. Acad. Sci. USA. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staeheli, T.I.2    Gordon, J.3
  • 38
    • 0024785542 scopus 로고
    • Purification and isolation of choline acetyltransferase from the electric organ of Torpedo marmorata by affinity chromatography
    • Waser G., Riggio G. and Raeber A. J. (1989), Purification and isolation of choline acetyltransferase from the electric organ of Torpedo marmorata by affinity chromatography. Eur. J. Biochem. 186, 487-492.
    • (1989) Eur. J. Biochem. , vol.186 , pp. 487-492
    • Waser, G.1    Riggio, G.2    Raeber, A.J.3
  • 39
    • 0023077419 scopus 로고
    • Cholinergic synaptic vesicles from the electromotor nerve terminals of Torpedo. Composition and life cycle
    • Whittaker V. P. (1987), Cholinergic synaptic vesicles from the electromotor nerve terminals of Torpedo. Composition and life cycle. Ann. N. Y. Acad. Sci. 493, 77-91.
    • (1987) Ann. N. Y. Acad. Sci. , vol.493 , pp. 77-91
    • Whittaker, V.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.