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Volumn 28, Issue 2, 2004, Pages 61-70

Cholinesterase inhibitory activities of the scorpion Mesobuthus gibbosus (Buthidae) venom peptides

Author keywords

Acetylcholinesterase; Buthidae; Butyrylcholinesterase; Inhibition; Mesobuthus gibbosus

Indexed keywords

AMINE; CHOLINESTERASE; ENZYME; ION CHANNEL; NEUROTOXIN; PEPTIDE DERIVATIVE; PROTEINASE; SCORPION VENOM; SEPHADEX;

EID: 2942706113     PISSN: 13004182     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (12)

References (40)
  • 1
    • 0027948873 scopus 로고
    • Diversity and endemism in tropical versus temperate scorpion communities
    • Lourenco WR. Diversity and endemism in tropical versus temperate scorpion communities, Biogiographica, 70, 155-160, 1994.
    • (1994) Biogiographica , vol.70 , pp. 155-160
    • Lourenco, W.R.1
  • 3
    • 0142056149 scopus 로고    scopus 로고
    • Primary structure and electrophysiological characterization of two almost identical isoforms of toxin from Isometrus vittatus (family: Buthidae) scorpion venom
    • Coronas FV, Stankiewichz M, Batiata CVP, Giraud S, Alam JM, Possan, LD, Mebs D, Pelhate M. Primary structure and electrophysiological characterization of two almost identical isoforms of toxin from Isometrus vittatus (family: Buthidae) scorpion venom, Toxicon, 41, 989-997, 2003.
    • (2003) Toxicon , vol.41 , pp. 989-997
    • Coronas, F.V.1    Stankiewichz, M.2    Batiata, C.V.P.3    Giraud, S.4    Alam, J.M.5    Possan, L.D.6    Mebs, D.7    Pelhate, M.8
  • 4
    • 0037401417 scopus 로고    scopus 로고
    • Purification and characterization of a thrombin like enzyme, elegaxobin II, with lysbradykinin releasing activity from the venom of Trimeresurus elegans (Sakishima-Habu)
    • Oyama E, Takahashi H. Purification and characterization of a thrombin like enzyme, elegaxobin II, with lysbradykinin releasing activity from the venom of Trimeresurus elegans (Sakishima-Habu), Toxicon, 41, 559-568, 2003.
    • (2003) Toxicon , vol.41 , pp. 559-568
    • Oyama, E.1    Takahashi, H.2
  • 6
    • 0033742266 scopus 로고    scopus 로고
    • Peptides and genes coding for scorpion toxins that affect ion-channels
    • Possani LD, Merino E, Corona M, Bolivar F, Becerril B. Peptides and genes coding for scorpion toxins that affect ion-channels, Biochimie, 82, 861-868, 2000.
    • (2000) Biochimie , vol.82 , pp. 861-868
    • Possani, L.D.1    Merino, E.2    Corona, M.3    Bolivar, F.4    Becerril, B.5
  • 9
    • 0027994580 scopus 로고
    • Scorpion sting-induced pulmonary edema: Evidence of alveolocapillary membrane permeability
    • Amaral CSF, Barbosa AIA, Leite VHR, Tafuri WL, De Resende NA. Scorpion sting-induced pulmonary edema: evidence of alveolocapillary membrane permeability, Toxicon, 32, 999-1003, 1994.
    • (1994) Toxicon , vol.32 , pp. 999-1003
    • Amaral, C.S.F.1    Barbosa, A.I.A.2    Leite, V.H.R.3    Tafuri, W.L.4    De Resende, N.A.5
  • 10
    • 0001252084 scopus 로고    scopus 로고
    • Inflammatory cytokines and scorpion envenomation: Analysis of serological levels in 46 Tunisian patients
    • Barbouche MR, Haguiga H, Nouira S, Krifi MN, Abroug F, Bouchoucha S, Dellagi K. Inflammatory cytokines and scorpion envenomation: analysis of serological levels in 46 Tunisian patients, Toxicon, 34, 156, 1996.
    • (1996) Toxicon , vol.34 , pp. 156
    • Barbouche, M.R.1    Haguiga, H.2    Nouira, S.3    Krifi, M.N.4    Abroug, F.5    Bouchoucha, S.6    Dellagi, K.7
  • 11
    • 0037355446 scopus 로고    scopus 로고
    • Relationship between plasmatic levels of various cytokines, tumour necrosis factor, enzymes, glucose and venom concentration following Tityus scorpion sting
    • D'Suze G, Moncada S, González C, Sevcik C, Aguilar V, Alagon A. Relationship between plasmatic levels of various cytokines, tumour necrosis factor, enzymes, glucose and venom concentration following Tityus scorpion sting, Toxicon, 41, 367-375, 2003.
    • (2003) Toxicon , vol.41 , pp. 367-375
    • D'Suze, G.1    Moncada, S.2    González, C.3    Sevcik, C.4    Aguilar, V.5    Alagon, A.6
  • 12
    • 0037212642 scopus 로고    scopus 로고
    • Increased plasma levels of IL-1β, IL-6, IL-8, IL-10 and TNF-α in patients moderately or severely envenomed by Tityus serrulatus scorpion sting
    • Fukuhara YDM, Reis ML, Dellalibera-Joviliano R, Cunha FQC, Donadi EA. Increased plasma levels of IL-1β, IL-6, IL-8, IL-10 and TNF-α in patients moderately or severely envenomed by Tityus serrulatus scorpion sting, Toxicon, 41(1), 49-55, 2003.
    • (2003) Toxicon , vol.41 , Issue.1 , pp. 49-55
    • Fukuhara, Y.D.M.1    Reis, M.L.2    Dellalibera-Joviliano, R.3    Cunha, F.Q.C.4    Donadi, E.A.5
  • 13
    • 0027142556 scopus 로고
    • Cytokine patterns in patients after major vascular surgery, hemorrhagic shock and severe blunt trauma: Relation with subsequent adult respiratory distress syndrome and multiple organ failure
    • Roumen RMH, Hendriks T, Vander-Ven-Jongekrijg J. Cytokine patterns in patients after major vascular surgery, hemorrhagic shock and severe blunt trauma: relation with subsequent adult respiratory distress syndrome and multiple organ failure, Am. Surg., 218, 769-775, 1993.
    • (1993) Am. Surg. , vol.218 , pp. 769-775
    • Roumen, R.M.H.1    Hendriks, T.2    Vander-Ven-Jongekrijg, J.3
  • 14
    • 0032217038 scopus 로고    scopus 로고
    • 1-antitrypsin in scorpion envenomed children
    • 1-antitrypsin in scorpion envenomed children, Toxicon, 36, 1851-1859, 1998.
    • (1998) Toxicon , vol.36 , pp. 1851-1859
    • Meki, A.R.M.A.1    Mohey-Eldean, Z.M.2
  • 15
    • 0001898094 scopus 로고
    • Die Skorpione der Ägäis, Beiträge zur Systematik, Phylogenie und Biogeographie
    • Kinzelbach R. Die Skorpione der Ägäis, Beiträge zur Systematik, Phylogenie und Biogeographie. Zool. Jahrb. (Syst.), 102, 12-50, 1975.
    • (1975) Zool. Jahrb. (Syst.) , vol.102 , pp. 12-50
    • Kinzelbach, R.1
  • 16
    • 0042723691 scopus 로고    scopus 로고
    • The scorpions (Arachnida: Scorpiones) of the Aegean area: Current problems in taxonomy and biogeography
    • Fet V, Braunwalder ME. The scorpions (Arachnida: Scorpiones) of the Aegean area: current problems in taxonomy and biogeography, Belg. J. Zool., 130 (Suppl 1), 17-22, 2000.
    • (2000) Belg. J. Zool. , vol.130 , Issue.SUPPL. 1 , pp. 17-22
    • Fet, V.1    Braunwalder, M.E.2
  • 18
    • 0343416891 scopus 로고    scopus 로고
    • Amitriptyline: A potent inhibitor of butyrylcholinesterase from human serum
    • Cokugras AN, Tezcan F. Amitriptyline: a potent inhibitor of butyrylcholinesterase from human serum, Gen. Pharmacol., 29, 835-838, 1997.
    • (1997) Gen. Pharmacol. , vol.29 , pp. 835-838
    • Cokugras, A.N.1    Tezcan, F.2
  • 19
    • 0028818897 scopus 로고
    • Aceytlchoiinesterase inhibition by fasciculine: Crystal structure of the complex
    • Bourne Y, Taylor P, Marchot P. Aceytlchoiinesterase inhibition by fasciculine: crystal structure of the complex, Cell, 83, 503-512, 1995.
    • (1995) Cell , vol.83 , pp. 503-512
    • Bourne, Y.1    Taylor, P.2    Marchot, P.3
  • 21
  • 23
    • 0030740563 scopus 로고    scopus 로고
    • Enzymatic properties of the Duvernoy's secretion of blanding's tree snake (Boiga blandingi) and of the mangrove snake (Boiga dendrophila)
    • Broaders M, Ryan MF. Enzymatic properties of the Duvernoy's secretion of blanding's tree snake (Boiga blandingi) and of the mangrove snake (Boiga dendrophila), Toxicon, 35(7), 1143-1148, 1997.
    • (1997) Toxicon , vol.35 , Issue.7 , pp. 1143-1148
    • Broaders, M.1    Ryan, M.F.2
  • 24
    • 0025807903 scopus 로고
    • A comparative study of the biological properties of Dendroaspis (mamba) snake venoms
    • Tan NH, Ponnudurai G. A comparative study of the biological properties of Dendroaspis (mamba) snake venoms, Comp. Biochem. Physiol., 99C, 463-466, 1991.
    • (1991) Comp. Biochem. Physiol. , vol.99 C , pp. 463-466
    • Tan, N.H.1    Ponnudurai, G.2
  • 25
    • 0342618344 scopus 로고    scopus 로고
    • Synthetic peptides derived from the central loop of fasciculin: Structural analysis and evaluation as inhibitors of acetylcholinesterase
    • Falkenstein RJ, Pena C. Synthetic peptides derived from the central loop of fasciculin: structural analysis and evaluation as inhibitors of acetylcholinesterase, Biochim. Biophys. Acta, 1340, 143-151, 1997.
    • (1997) Biochim. Biophys. Acta , vol.1340 , pp. 143-151
    • Falkenstein, R.J.1    Pena, C.2
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of the head of the bacteriophage T4
    • Laemmli UK. Cleavage of structural protein during the assembly of the head of the bacteriophage T4, Nature, 227, 680-685, 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0026561123 scopus 로고
    • Age-correlated modifications of copper-zinc superoxide dismutase and glutathione-related enzyme activities in human erythrocytes
    • Ceballos-Picot I, Trivier JV, Nicole A, Sinet PM, Thevenin M. Age-correlated modifications of copper-zinc superoxide dismutase and glutathione-related enzyme activities in human erythrocytes, Clin. Chem., 38(1), 66-70, 1992.
    • (1992) Clin. Chem. , vol.38 , Issue.1 , pp. 66-70
    • Ceballos-Picot, I.1    Trivier, J.V.2    Nicole, A.3    Sinet, P.M.4    Thevenin, M.5
  • 30
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H, Burk D. The determination of enzyme dissociation constants, J. Am. Chem. Soc., 56, 658-666, 1934.
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 31
    • 0003518480 scopus 로고
    • Wiley-Interscience Publication, New York
    • Segel IH. Enzyme Kinetics, Wiley-Interscience Publication, New York, 125-135, 1975.
    • (1975) Enzyme Kinetics , pp. 125-135
    • Segel, I.H.1
  • 32
    • 0034894415 scopus 로고    scopus 로고
    • Characterization of the gene encoding the α-toxin Amm V from the scorpion Androctonus mauretonicus mauretanicus
    • Alami M, Ouafik L, Céard B, Legros C, Bougis PE, Martin-Eauclaire M. Characterization of the gene encoding the α-toxin Amm V from the scorpion Androctonus mauretonicus mauretanicus, Toxicon, 39, 1579-1585, 2001.
    • (2001) Toxicon , vol.39 , pp. 1579-1585
    • Alami, M.1    Ouafik, L.2    Céard, B.3    Legros, C.4    Bougis, P.E.5    Martin-Eauclaire, M.6
  • 33
    • 0034594361 scopus 로고    scopus 로고
    • The isolation and purification of two peptides from the venom of Buthus martensii Karsh
    • Chen Z, Reddy G, Hahin R. The isolation and purification of two peptides from the venom of Buthus martensii Karsh, Toxicon, 38, 1817-1832, 2000.
    • (2000) Toxicon , vol.38 , pp. 1817-1832
    • Chen, Z.1    Reddy, G.2    Hahin, R.3
  • 34
    • 0035401349 scopus 로고    scopus 로고
    • Purification, amino-acid sequence and partial characterization of two toxins with anti-insect activity from the venom of the South American scorpion Tityus bahiensis (Buthidae)
    • Pimenta AMC, Martin-Eauclaire M, Rochat H, Figueiredo SG, Kalapothakis E, Afonso LCC, De Lima ME. Purification, amino-acid sequence and partial characterization of two toxins with anti-insect activity from the venom of the South American scorpion Tityus bahiensis (Buthidae), Toxicon, 39, 1009-1019, 2001.
    • (2001) Toxicon , vol.39 , pp. 1009-1019
    • Pimenta, A.M.C.1    Martin-Eauclaire, M.2    Rochat, H.3    Figueiredo, S.G.4    Kalapothakis, E.5    Afonso, L.C.C.6    De Lima, M.E.7
  • 36
  • 37
    • 0036096678 scopus 로고    scopus 로고
    • Separation and purification of Echis coloratus venom and some biological and biochemical effects of the proteins
    • AI-Saleh SS, Ghneim HK, Haddad HY, Khan SU. Separation and purification of Echis coloratus venom and some biological and biochemical effects of the proteins, Cell Biochem. Funct., 20, 153-162, 2002.
    • (2002) Cell Biochem. Funct. , vol.20 , pp. 153-162
    • Ai-Saleh, S.S.1    Ghneim, H.K.2    Haddad, H.Y.3    Khan, S.U.4
  • 38
    • 0142039868 scopus 로고    scopus 로고
    • Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products
    • Nicolet Y, Lockridge O, Masson P, Fontecilla-Camps, JC, Nachon F. Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products, J. Biol. Chem., 278 (42), 41141-41147, 2003.
    • (2003) J. Biol. Chem. , vol.278 , Issue.42 , pp. 41141-41147
    • Nicolet, Y.1    Lockridge, O.2    Masson, P.3    Fontecilla-Camps, J.C.4    Nachon, F.5
  • 39
    • 0033524414 scopus 로고    scopus 로고
    • Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis: Substrate inhibition arises as a secondary effect
    • Szegletes T, Mallander WD, Thomas PJ, Rosenberry TL. Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis: substrate inhibition arises as a secondary effect, Biochemistry, 38, 122-133, 1999.
    • (1999) Biochemistry , vol.38 , pp. 122-133
    • Szegletes, T.1    Mallander, W.D.2    Thomas, P.J.3    Rosenberry, T.L.4
  • 40
    • 0029133139 scopus 로고
    • Allosteric control of acetylcholinesterase catalysis by fasciculin
    • Radic Z, Quinn DM, Vellom DC, Camp S, Taylor P. Allosteric control of acetylcholinesterase catalysis by fasciculin, J. Biol. Chem., 270 (35), 20391-20399, 1995.
    • (1995) J. Biol. Chem. , vol.270 , Issue.35 , pp. 20391-20399
    • Radic, Z.1    Quinn, D.M.2    Vellom, D.C.3    Camp, S.4    Taylor, P.5


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