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Volumn 218, Issue 1, 2010, Pages 1-5

Localization and properties of cholinesterases in the common prawn (Palaemon serratus): A Kinetic-histochemical study

Author keywords

[No Author keywords available]

Indexed keywords

BIOMARKER; CRUSTACEAN; ENZYME ACTIVITY; ESTER; FUNCTIONAL MORPHOLOGY; HISTOLOGY; INHIBITION; INHIBITOR; MUSCLE; PERFORMANCE ASSESSMENT; PESTICIDE; REACTION KINETICS; SENSITIVITY ANALYSIS; SPECIES DIVERSITY;

EID: 77952300981     PISSN: 00063185     EISSN: None     Source Type: Journal    
DOI: 10.1086/BBLv218n1p1     Document Type: Article
Times cited : (5)

References (32)
  • 2
    • 0033839291 scopus 로고    scopus 로고
    • The use of cholinesterase activity in flounder (Platichthys flesus) muscle tissue as a biomarker of neurotoxic contamination in UK estuaries
    • Kirby, M. F., S. Morris, M. Hurst, S. J. Kirby, P. Neall, T. Tylor, and A. Fagg. 2000. The use of cholinesterase activity in flounder (Platichthys flesus) muscle tissue as a biomarker of neurotoxic contamination in UK estuaries. Mar. Pollut. Bull. 40: 780-791.
    • (2000) Mar. Pollut. Bull. , vol.40 , pp. 780-791
    • Kirby, M.F.1    Morris, S.2    Hurst, M.3    Kirby, S.J.4    Neall, P.5    Tylor, T.6    Fagg, A.7
  • 3
    • 0037433103 scopus 로고    scopus 로고
    • Acetylcholinesterase activity in copepods (Tigriopus brevicornis) from the Vilaine River estuary, France, as a biomarker of neurotoxic contaminants
    • Forget, J., B. Beliaeff, and G. Bocquené. 2003. Acetylcholinesterase activity in copepods (Tigriopus brevicornis) from the Vilaine River estuary, France, as a biomarker of neurotoxic contaminants. Aquat. Toxicol. 62: 195-204.
    • (2003) Aquat. Toxicol. , vol.62 , pp. 195-204
    • Forget, J.1    Beliaeff, B.2    Bocquené, G.3
  • 4
    • 0036087674 scopus 로고    scopus 로고
    • Environmental, biological, and methodological factors affecting cholinesterase activity in walleye (Stizostedion vitreum)
    • Phillips, T. A., R. C. Summerfelt, and G. J. Atchison. 2002. Environmental, biological, and methodological factors affecting cholinesterase activity in walleye (Stizostedion vitreum). Arch. Environ. Contam. Toxicol. 43: 75-80.
    • (2002) Arch. Environ. Contam. Toxicol. , vol.43 , pp. 75-80
    • Phillips, T.A.1    Summerfelt, R.C.2    Atchison, G.J.3
  • 5
    • 0242319047 scopus 로고    scopus 로고
    • Intraclonal variability in Daphnia acetylcholinesterase activity: The implications for its applicability as a biomarker
    • Printes, L. B., and A. Callaghan. 2003. Intraclonal variability in Daphnia acetylcholinesterase activity: the implications for its applicability as a biomarker. Environ. Toxicol. Chem. 22: 2042-2047.
    • (2003) Environ. Toxicol. Chem. , vol.22 , pp. 2042-2047
    • Printes, L.B.1    Callaghan, A.2
  • 6
    • 0030940939 scopus 로고    scopus 로고
    • Cholinesterases from the common oyster (Crassostrea gigas). Evidence for the presence of a soluble acetylcholinesterase insensitive to organophosphate and carbamate inhibitors
    • Bocquené, G., A. Roig, and D. Fournier. 1997. Cholinesterases from the common oyster (Crassostrea gigas). Evidence for the presence of a soluble acetylcholinesterase insensitive to organophosphate and carbamate inhibitors. FEBS Lett. 407: 261-266.
    • (1997) FEBS Lett , vol.407 , pp. 261-266
    • Bocquené, G.1    Roig, A.2    Fournier, D.3
  • 7
    • 0034041109 scopus 로고    scopus 로고
    • Different sensitivity to organophosphates of acetylcholinesterase and butyryl- cholinesterase from three-spined stickleback (Gasterosteus aculeatus): Application in biomonitoring
    • Sturm, A., J. Wogram, H. Segner, and M. Liess. 2000. Different sensitivity to organophosphates of acetylcholinesterase and butyryl- cholinesterase from three-spined stickleback (Gasterosteus aculeatus): Application in biomonitoring. Environ. Toxicol. Chem. 19: 1607-1615.
    • (2000) Environ. Toxicol. Chem. , vol.19 , pp. 1607-1615
    • Sturm, A.1    Wogram, J.2    Segner, H.3    Liess, M.4
  • 8
    • 0034826911 scopus 로고    scopus 로고
    • Acetyl-cholinesterase of Mytilus galloprovincialis Lmk: Hemolymph: A suitable environmental biomarker
    • Moreira, S. M., J. Coimbra, and L. Guilhermino. 2001. Acetyl-cholinesterase of Mytilus galloprovincialis Lmk: Hemolymph: A suitable environmental biomarker. Bull. Environ. Contam. Toxicol. 67: 470-475.
    • (2001) Bull. Environ. Contam. Toxicol. , vol.67 , pp. 470-475
    • Moreira, S.M.1    Coimbra, J.2    Guilhermino, L.3
  • 9
    • 17444373885 scopus 로고    scopus 로고
    • Sea-urchin (Paracentrotus lividus) glutathione S-transferases and cholinesterase activities as biomarkers of environmental contamination
    • Cunha, I., L. M. García, and L. Guilhermino. 2005. Sea-urchin (Paracentrotus lividus) glutathione S-transferases and cholinesterase activities as biomarkers of environmental contamination. J. Environ. Monit. 7: 288-294.
    • (2005) J. Environ. Monit. , vol.7 , pp. 288-294
    • Cunha, I.1    García, L.M.2    Guilhermino, L.3
  • 10
    • 0028991662 scopus 로고
    • Joint action of combinations of pollutants on the acetylcholinesterase activity of several marine species
    • BocquenéG., C. Bellanger, Y. Cadiou, and F. Galgani. 1995. Joint action of combinations of pollutants on the acetylcholinesterase activity of several marine species. Ecotoxicology 4: 266 -279.
    • (1995) Ecotoxicology , vol.4 , pp. 266-279
    • Bocquené, G.1    Bellanger, C.2    Cadiou, Y.3    Galgani, F.4
  • 11
    • 0034489462 scopus 로고    scopus 로고
    • Population characteristics of the prawn Palaemon serratus (Decapoda, Palaemonidae) in a shallow Mediterranean bay
    • Guerao, G., and C. Ribera. 2000. Population characteristics of the prawn Palaemon serratus (Decapoda, Palaemonidae) in a shallow Mediterranean bay. Crustaceana 73: 459-468.
    • (2000) Crustaceana , vol.73 , pp. 459-468
    • Guerao, G.1    Ribera, C.2
  • 12
    • 33646470860 scopus 로고    scopus 로고
    • Cholinesterase from the common prawn (Palaemon serratus) eyes: Catalytic properties and sensitivity to organophosphate and car- bamate compounds
    • Frasco, M. F., D. Fournier, F. Carvalho, and L. Guilhermino. 2006. Cholinesterase from the common prawn (Palaemon serratus) eyes: Catalytic properties and sensitivity to organophosphate and car- bamate compounds. Aquat. Toxicol. 77: 412-421.
    • (2006) Aquat. Toxicol. , vol.77 , pp. 412-421
    • Frasco, M.F.1    Fournier, D.2    Carvalho, F.3    Guilhermino, L.4
  • 13
    • 23744453157 scopus 로고    scopus 로고
    • A short-term sublethal in situ toxicity assay with Hediste diversicolor (Polychaeta) for estuarine sediments based on post- exposure feeding
    • Moreira, S. M., M. Moreira-Santos, L. Guilhermino, and R. Ribeiro. 2005. A short-term sublethal in situ toxicity assay with Hediste diversicolor (Polychaeta) for estuarine sediments based on post- exposure feeding. Environ. Toxicol. Chem. 24: 2010-2018.
    • (2005) Environ. Toxicol. Chem. , vol.24 , pp. 2010-2018
    • Moreira, S.M.1    Moreira-Santos, M.2    Guilhermino, L.3    Ribeiro, R.4
  • 14
    • 33751329718 scopus 로고    scopus 로고
    • Impact of chemical exposure on the fish Pomatoschistus microps Kr0yer (1838) in estuaries of the Portuguese Northwest coast
    • Monteiro, M., C. Quintaneiro, A. J. A. Nogueira, F. Morgado, A. M. V. M. Soares, and L. Guilhermino. 2007. Impact of chemical exposure on the fish Pomatoschistus microps Kr0yer (1838) in estuaries of the Portuguese Northwest coast. Chemosphere 66: 514-522.
    • (2007) Chemosphere , vol.66 , pp. 514-522
    • Monteiro, M.1    Quintaneiro, C.2    Nogueira, A.J.A.3    Morgado, F.4    Soares, A.M.V.M.5    Guilhermino, L.6
  • 15
    • 78651153462 scopus 로고
    • A "direct-coloring" thio-choline method for cholinesterases
    • Karnovsky, M. J., and L. Roots. 1964. A "direct-coloring" thio-choline method for cholinesterases. J. Histochem. Cytochem. 12: 219-221.
    • (1964) J. Histochem. Cytochem. , vol.12 , pp. 219-221
    • Karnovsky, M.J.1    Roots, L.2
  • 16
    • 33644811612 scopus 로고
    • A new and rapid colorimetric determination of acetylcholines- terase activity
    • Ellman, G. L., K. D. Courtney, V. Andres, and R. M. Featherstone. 1961. A new and rapid colorimetric determination of acetylcholines- terase activity. Biochem. Pharmacol. 7: 88-95.
    • (1961) Biochem. Pharmacol. , vol.7 , pp. 88-95
    • Ellman, G.L.1    Courtney, K.D.2    Andres, V.3    Featherstone, R.M.4
  • 17
    • 0034307502 scopus 로고    scopus 로고
    • A method to estimate acetylcholinesterase-active sites and turnover in insects
    • Charpentier, A., P. Menozzi, V. Marcel, F. Villatte, and D. Fournier. 2000. A method to estimate acetylcholinesterase-active sites and turnover in insects. Anal. Biochem. 285: 76-81.
    • (2000) Anal. Biochem. , vol.285 , pp. 76-81
    • Charpentier, A.1    Menozzi, P.2    Marcel, V.3    Villatte, F.4    Fournier, D.5
  • 18
    • 1942520265 scopus 로고    scopus 로고
    • Inhibition of Drosophila melanogaster acetylcholinesterase by high concentrations of substrate
    • Stojan, J., L. Brochier, C. Alies, J.-P. Colletier, and D. Fournier. 2004. Inhibition of Drosophila melanogaster acetylcholinesterase by high concentrations of substrate. Eur. J. Biochem. 271: 1364-1371.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1364-1371
    • Stojan, J.1    Brochier, L.2    Alies, C.3    Colletier, J.-P.4    Fournier, D.5
  • 19
    • 33847131863 scopus 로고    scopus 로고
    • Cell signaling during sea urchin development: A model for assessing toxicity of environmental contaminants
    • Angelini, C., M. G. Aluigi, M. Sgro, H. Trombino, H. Thielecke, and C. Falugi. 2005. Cell signaling during sea urchin development: A model for assessing toxicity of environmental contaminants. Prog. Mol. Subcell. Biol. 39: 45-70.
    • (2005) Prog. Mol. Subcell. Biol. , vol.39 , pp. 45-70
    • Angelini, C.1    Aluigi, M.G.2    Sgro, M.3    Trombino, H.4    Thielecke, H.5    Falugi, C.6
  • 20
    • 0037290117 scopus 로고    scopus 로고
    • Biological targets of neurotoxic pesticides analysed by alteration of developmental events in the Mediterranean sea urchin, Paracentrotus lividus
    • Pesando, D., P. Huitorel, V. Dolcini, C. Angelini, P. Guidetti, and C. Falugi. 2003. Biological targets of neurotoxic pesticides analysed by alteration of developmental events in the Mediterranean sea urchin, Paracentrotus lividus. Mar. Environ. Res. 55: 39-57.
    • (2003) Mar. Environ. Res. , vol.55 , pp. 39-57
    • Pesando, D.1    Huitorel, P.2    Dolcini, V.3    Angelini, C.4    Guidetti, P.5    Falugi, C.6
  • 21
    • 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., M. Grauso, E. Giovannini, G. Rosi, and J.-P. Toutant. 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
  • 22
    • 0032142768 scopus 로고    scopus 로고
    • Acetylcholinesterase at high catalytic efficiency and substrate specificity in the optic lobe of Eledone moschata (Cephalopoda: Oc-topoda): Biochemical characterization and histochemical localization
    • Talesa, V., R. Romani, M. Calvitti, G. Rosi, and E. Giovannini. 1998. Acetylcholinesterase at high catalytic efficiency and substrate specificity in the optic lobe of Eledone moschata (Cephalopoda: Oc-topoda): Biochemical characterization and histochemical localization. Neurochem. Int. 33: 131-141.
    • (1998) Neurochem. Int. , vol.33 , pp. 131-141
    • Talesa, V.1    Romani, R.2    Calvitti, M.3    Rosi, G.4    Giovannini, E.5
  • 23
    • 0015819225 scopus 로고
    • Localization and properties of the cholinesterase in crustacean muscle
    • Spielholz, N.I., and W. G. Van der Kloot. 1973. Localization and properties of the cholinesterase in crustacean muscle. J. Cell. Biol. 59: 407-420.
    • (1973) J. Cell. Biol. , vol.59 , pp. 407-420
    • Spielholz, N.I.1    Van Der Kloot, W.G.2
  • 24
    • 0025049104 scopus 로고
    • Characterization and assay conditions for use of AChE activity from several marine species in pollution monitoring
    • Bocquené, G., F. Galgani, and P. Truquet. 1990. Characterization and assay conditions for use of AChE activity from several marine species in pollution monitoring. Mar. Environ. Res. 30: 75-89.
    • (1990) Mar. Environ. Res. , vol.30 , pp. 75-89
    • Bocquené, G.1    Galgani, F.2    Truquet, P.3
  • 25
    • 0026320617 scopus 로고
    • Acetylcholinesterase activity in the common prawn (Palaemon serratus) contaminated by carbaryl and phosalone: Choice of a method for detection of effects
    • Bocquené, G., and F. Galgani. 1991. Acetylcholinesterase activity in the common prawn (Palaemon serratus) contaminated by carbaryl and phosalone: Choice of a method for detection of effects. Ecotoxicol. Environ. Saf. 22: 337-344.
    • (1991) Ecotoxicol. Environ. Saf. , vol.22 , pp. 337-344
    • Bocquené, G.1    Galgani, F.2
  • 26
    • 0031706994 scopus 로고    scopus 로고
    • Some kinetic and tox-icological characteristics of thoracic ganglia cholinesterase of Chas-magnathus granulata (Decapoda, Grapsidae)
    • Monserrat, J. M., and A. Bianchini. 1998. Some kinetic and tox-icological characteristics of thoracic ganglia cholinesterase of Chas-magnathus granulata (Decapoda, Grapsidae). Comp. Biochem. Physiol. C 120: 193-199.
    • (1998) Comp. Biochem. Physiol. C , vol.120 , pp. 193-199
    • Monserrat, J.M.1    Bianchini, A.2
  • 27
    • 0032828083 scopus 로고    scopus 로고
    • Partial purification and enzymatic characterization of acetylcholinesterase from the intertidal marine copepod Tigriopus brevicornis
    • Forget, J., and G. Bocquené. 1999. Partial purification and enzymatic characterization of acetylcholinesterase from the intertidal marine copepod Tigriopus brevicornis. Comp. Biochem. Physiol. B 123: 345-350.
    • (1999) Comp. Biochem. Physiol. B , vol.123 , pp. 345-350
    • Forget, J.1    Bocquené, G.2
  • 28
    • 0036258955 scopus 로고    scopus 로고
    • Partial purification and characterization of acetylcholinesterase (AChE) from the estuarine copepod Eurytemora affinis (Poppe)
    • Forget, J., S. Livet, and F. Leboulenger. 2002. Partial purification and characterization of acetylcholinesterase (AChE) from the estuarine copepod Eurytemora affinis (Poppe). Comp. Biochem. Physiol. C 132: 85-92.
    • (2002) Comp. Biochem. Physiol. C , vol.132 , pp. 85-92
    • Forget, J.1    Livet, S.2    Leboulenger, F.3
  • 29
    • 0036290021 scopus 로고    scopus 로고
    • Characterization of cholines- terase activity in tissues of the grass shrimp (Palaemonetes pugio)
    • Key, P. B., and M. H. Fulton. 2002. Characterization of cholines- terase activity in tissues of the grass shrimp (Palaemonetes pugio). Pestic. Biochem. Physiol. 72: 186-192.
    • (2002) Pestic. Biochem. Physiol. , vol.72 , pp. 186-192
    • Key, P.B.1    Fulton, M.H.2
  • 32
    • 0035987529 scopus 로고    scopus 로고
    • Characterisation of cholinesterases and evaluation of the inhibitory potential of chlorpyrifos and dichlorvos to Artemia salina and Artemia parthenogenetica
    • Varó , I., J. C. Navarro, F. Amat, and L. Guilhermino. 2002. Characterisation of cholinesterases and evaluation of the inhibitory potential of chlorpyrifos and dichlorvos to Artemia salina and Artemia parthenogenetica. Chemosphere 48: 563-569.
    • (2002) Chemosphere , vol.48 , pp. 563-569
    • Varó, I.1    Navarro, J.C.2    Amat, F.3    Guilhermino, L.4


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