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Volumn 152, Issue 1-2, 2008, Pages 116-126

Molecular cloning, expression and characterization of a functional GSTmu class from the cattle tick Boophilus annulatus

Author keywords

B. annulatus; Cattle ticks; Class mu; Cloning; Glutathine S transferase

Indexed keywords

1 CHLORO 2,4 DINITROBENZENE; BETA GALACTOSIDASE; GLUTATHIONE TRANSFERASE;

EID: 38749140598     PISSN: 03044017     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.vetpar.2007.12.014     Document Type: Article
Times cited : (24)

References (48)
  • 1
    • 33646051960 scopus 로고    scopus 로고
    • Studies on Glutathione transferase from grasshopper (Zonocerus variegatus)
    • Adewale I.O., and Afolayan A. Studies on Glutathione transferase from grasshopper (Zonocerus variegatus). Pestic. Biochem. Physiol. 85 (2006) 52-59
    • (2006) Pestic. Biochem. Physiol. , vol.85 , pp. 52-59
    • Adewale, I.O.1    Afolayan, A.2
  • 3
    • 0003198468 scopus 로고    scopus 로고
    • Structure, mechanism and evolution of thiol transferases
    • Armstrong R.N., Rife C., and Wang Z. Structure, mechanism and evolution of thiol transferases. Chem. Biol. Interact. 133 (2001) 167-169
    • (2001) Chem. Biol. Interact. , vol.133 , pp. 167-169
    • Armstrong, R.N.1    Rife, C.2    Wang, Z.3
  • 4
    • 0033226367 scopus 로고    scopus 로고
    • Detecting resistance to organophosphates and carbamates in the cattle tick Boophilus microplus, with a propoxur-based biochemical test
    • Baxter G.D., Green P., Stuttgen M., and Baker S.C. Detecting resistance to organophosphates and carbamates in the cattle tick Boophilus microplus, with a propoxur-based biochemical test. Exp. Appl. Acarol. 23 11 (1999) 907-914
    • (1999) Exp. Appl. Acarol. , vol.23 , Issue.11 , pp. 907-914
    • Baxter, G.D.1    Green, P.2    Stuttgen, M.3    Baker, S.C.4
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0024488993 scopus 로고
    • The comparative enzymology of the glutathione S-transferases from non-vertebrate organisms
    • Clark A.G. The comparative enzymology of the glutathione S-transferases from non-vertebrate organisms. Comp. Biochem. Physiol. B 92 3 (1989) 419-446
    • (1989) Comp. Biochem. Physiol. B , vol.92 , Issue.3 , pp. 419-446
    • Clark, A.G.1
  • 8
    • 0034486265 scopus 로고    scopus 로고
    • Immunization of cross-bred cattle against Hyalomma anatolicum anatolicum by purified antigens
    • Das G., Ghosh S., Khan M.H., and Sharma J.K. Immunization of cross-bred cattle against Hyalomma anatolicum anatolicum by purified antigens. Exp. Appl. Acarol. 24 (2000) 645-659
    • (2000) Exp. Appl. Acarol. , vol.24 , pp. 645-659
    • Das, G.1    Ghosh, S.2    Khan, M.H.3    Sharma, J.K.4
  • 10
    • 33745654531 scopus 로고    scopus 로고
    • Strategies for development of vaccines for control of ixodid tick species
    • De La Fuente J., and Kocan K.M. Strategies for development of vaccines for control of ixodid tick species. Parasite Immunol. 28 (2006) 275-283
    • (2006) Parasite Immunol. , vol.28 , pp. 275-283
    • De La Fuente, J.1    Kocan, K.M.2
  • 11
    • 0033038758 scopus 로고    scopus 로고
    • Concise review of the glutathione S-tarnsferases and their significance to toxicity
    • Eaton D.L., and Bammler T.K. Concise review of the glutathione S-tarnsferases and their significance to toxicity. Toxicol. Sci. 49 (1999) 156-164
    • (1999) Toxicol. Sci. , vol.49 , pp. 156-164
    • Eaton, D.L.1    Bammler, T.K.2
  • 12
    • 0035040292 scopus 로고    scopus 로고
    • Glutathione S-transferases of Aulacorthum solani and Acyrthosiphon pisum: partial purification and characterization
    • Francis F., Haubruge E., Gaspar C., and Dierickx P.J. Glutathione S-transferases of Aulacorthum solani and Acyrthosiphon pisum: partial purification and characterization. Comp. Biochem. Physiol. B. Biochem. Mol. Biol. 129 1 (2001) 165-171
    • (2001) Comp. Biochem. Physiol. B. Biochem. Mol. Biol. , vol.129 , Issue.1 , pp. 165-171
    • Francis, F.1    Haubruge, E.2    Gaspar, C.3    Dierickx, P.J.4
  • 13
    • 0029257154 scopus 로고
    • Glutathione S-transferases in housefly (Musca domestica): location of GST-1 and GST-2 families
    • Franciosa H., and Berge J.B. Glutathione S-transferases in housefly (Musca domestica): location of GST-1 and GST-2 families. Insect Biochem. Mol. Biol. 25 3 (1995) 311-317
    • (1995) Insect Biochem. Mol. Biol. , vol.25 , Issue.3 , pp. 311-317
    • Franciosa, H.1    Berge, J.B.2
  • 14
    • 0033198377 scopus 로고    scopus 로고
    • Glutathione S-transferase from the spruce budworm, Choristoneura fumiferana: identification, characterization, localization, cDNA cloning, and expression
    • Feng Q.-L., Davey K.G., Pang A.S.D., Primavera M., Ladd T.R., Zheng S.C., Sohi S.S., Retnakaran A., and Palli S.R. Glutathione S-transferase from the spruce budworm, Choristoneura fumiferana: identification, characterization, localization, cDNA cloning, and expression. Insect Biochem. Mol. Biol. 29 9 (1999) 779-793
    • (1999) Insect Biochem. Mol. Biol. , vol.29 , Issue.9 , pp. 779-793
    • Feng, Q.-L.1    Davey, K.G.2    Pang, A.S.D.3    Primavera, M.4    Ladd, T.R.5    Zheng, S.C.6    Sohi, S.S.7    Retnakaran, A.8    Palli, S.R.9
  • 15
    • 0033208769 scopus 로고    scopus 로고
    • Cross-bred cattle protected against Hyalomma anatolicum anatolicum by larval antigens purified by immunoaffinity chromatography
    • Ghosh S., Khan M.H., and Ahmed N. Cross-bred cattle protected against Hyalomma anatolicum anatolicum by larval antigens purified by immunoaffinity chromatography. Trop. Anim. Health Prod. 33 (1999) 263-273
    • (1999) Trop. Anim. Health Prod. , vol.33 , pp. 263-273
    • Ghosh, S.1    Khan, M.H.2    Ahmed, N.3
  • 16
    • 0037106544 scopus 로고    scopus 로고
    • Cloning and expression of a novel Mu class murine glutathione transferase isoenzyme
    • Guo J., Zimniak L., Zimniak P., Orchard J.L., and Singh S.V. Cloning and expression of a novel Mu class murine glutathione transferase isoenzyme. Biochem. J. 366 Pt 3 (2002) 817-824
    • (2002) Biochem. J. , vol.366 , Issue.PART 3 , pp. 817-824
    • Guo, J.1    Zimniak, L.2    Zimniak, P.3    Orchard, J.L.4    Singh, S.V.5
  • 17
    • 0016275313 scopus 로고
    • Glutathione S-transferases. The first enzymatic step in mercapturic acid formation
    • Habig W.H., Pabst M.J., and Jakoby W.B. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249 22 (1974) 7130-7139
    • (1974) J. Biol. Chem. , vol.249 , Issue.22 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 18
    • 0033571041 scopus 로고    scopus 로고
    • An approach to optimizing the active site in glutathione transferase by evolution in vitro
    • Hansson L., Widersten M., and Mannervik B. An approach to optimizing the active site in glutathione transferase by evolution in vitro. Biochem. J. 344 1 (1999) 93-100
    • (1999) Biochem. J. , vol.344 , Issue.1 , pp. 93-100
    • Hansson, L.1    Widersten, M.2    Mannervik, B.3
  • 19
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • Hayes J.D., and Pulford D.J. The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit. Rev. Biochem. Mol. Biol. 30 (1995) 445-600
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 21
    • 0033179317 scopus 로고    scopus 로고
    • Characterization and molecular cloning of glutathione S-transferase gene from the tick, Boophilus microplus (Acari; Ixodidae)
    • He H., Chen A.C., Davey R.B., Ivie G.W., and George J.E. Characterization and molecular cloning of glutathione S-transferase gene from the tick, Boophilus microplus (Acari; Ixodidae). Insect Biochem. Mol. Biol. 29 (1999) 737-743
    • (1999) Insect Biochem. Mol. Biol. , vol.29 , pp. 737-743
    • He, H.1    Chen, A.C.2    Davey, R.B.3    Ivie, G.W.4    George, J.E.5
  • 23
    • 0032168783 scopus 로고    scopus 로고
    • Molecular cloning and heterologous expression of a glutathione S-transferase involved in insecticide resistance from the diamondback moth, Plutella xylostella
    • Huang H.S., Hu N.T., Yao Y.E., Wu C.Y., Chiang S.W., and Sun C.N. Molecular cloning and heterologous expression of a glutathione S-transferase involved in insecticide resistance from the diamondback moth, Plutella xylostella. Insect Biochem. Mol. Biol. 28 9 (1998) 651-658
    • (1998) Insect Biochem. Mol. Biol. , vol.28 , Issue.9 , pp. 651-658
    • Huang, H.S.1    Hu, N.T.2    Yao, Y.E.3    Wu, C.Y.4    Chiang, S.W.5    Sun, C.N.6
  • 24
    • 0035954627 scopus 로고    scopus 로고
    • Heterologous expression and characterization of alternatively spliced glutathione S-transferases from a single Anopheles gene
    • Jirajaroenrat K., Pongjaroenkit S., Krittanai C., Prapanthadara L., and Ketterman A.J. Heterologous expression and characterization of alternatively spliced glutathione S-transferases from a single Anopheles gene. Insect Biochem. Mol. Biol. 31 9 (2001) 867-875
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , Issue.9 , pp. 867-875
    • Jirajaroenrat, K.1    Pongjaroenkit, S.2    Krittanai, C.3    Prapanthadara, L.4    Ketterman, A.J.5
  • 25
    • 0026342613 scopus 로고
    • An analysis of vertebrate mRNA sequences: intimations of translational control
    • Kozak M. An analysis of vertebrate mRNA sequences: intimations of translational control. J. Cell Biol. 115 4 (1991) 887-903
    • (1991) J. Cell Biol. , vol.115 , Issue.4 , pp. 887-903
    • Kozak, M.1
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 5259 (1970) 680-685
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0000107746 scopus 로고
    • Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymztic properties
    • Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M., and Jornvall H. Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymztic properties. Proc. Natl. Acad. Sci. U.S.A. 82 (1985) 7202-7206
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 7202-7206
    • Mannervik, B.1    Alin, P.2    Guthenberg, C.3    Jensson, H.4    Tahir, M.K.5    Warholm, M.6    Jornvall, H.7
  • 29
    • 0001306237 scopus 로고
    • Human glutathione transferases: classification, tissue distribution, structure and functional properties
    • Pacifi G.M., and Fracchia G.N. (Eds), European Commission, Luxembourg
    • Mannervik B., and Widersten M. Human glutathione transferases: classification, tissue distribution, structure and functional properties. In: Pacifi G.M., and Fracchia G.N. (Eds). Advances in Drug Metabolism in Man (1995), European Commission, Luxembourg 407-459
    • (1995) Advances in Drug Metabolism in Man , pp. 407-459
    • Mannervik, B.1    Widersten, M.2
  • 32
    • 0028054012 scopus 로고
    • Cloning and characterization of a major allergen of the house dust mite, Dermatophagoides pteronyssinus, homologous with glutathione S-transferase
    • O'Neill G.M., Donovan G.R., and Baldo B.A. Cloning and characterization of a major allergen of the house dust mite, Dermatophagoides pteronyssinus, homologous with glutathione S-transferase. Biochem. Biophys. Acta 1219 2 (1994) 521-528
    • (1994) Biochem. Biophys. Acta , vol.1219 , Issue.2 , pp. 521-528
    • O'Neill, G.M.1    Donovan, G.R.2    Baldo, B.A.3
  • 33
    • 0030111457 scopus 로고    scopus 로고
    • Purification and characterization of a major glutathione S-transferase from the mosquito Anopheles dirus (species B)
    • Prapanthadara L.A., Koottathep S., Promtet N., Hemingway J., and Ketterman A.J. Purification and characterization of a major glutathione S-transferase from the mosquito Anopheles dirus (species B). Insect Biochem. Mol. Biol. Mar. 26 3 (1996) 277-285
    • (1996) Insect Biochem. Mol. Biol. Mar. , vol.26 , Issue.3 , pp. 277-285
    • Prapanthadara, L.A.1    Koottathep, S.2    Promtet, N.3    Hemingway, J.4    Ketterman, A.J.5
  • 34
    • 0017089669 scopus 로고
    • 3′ non-coding region sequences in eukaryotic messenger RNA
    • Proudfoot N.J., and Brownlee G.G. 3′ non-coding region sequences in eukaryotic messenger RNA. Nature 263 5574 (1976) 211-214
    • (1976) Nature , vol.263 , Issue.5574 , pp. 211-214
    • Proudfoot, N.J.1    Brownlee, G.G.2
  • 35
    • 0030917474 scopus 로고    scopus 로고
    • Cloning and characterization of two glutathione S-transferases from a DDT-resistant strain of Anopheles gambiae
    • Ranson H., Prapanthadara L.A., and Hemingway J. Cloning and characterization of two glutathione S-transferases from a DDT-resistant strain of Anopheles gambiae. Biochem. J. 324 1 (1997) 97-102
    • (1997) Biochem. J. , vol.324 , Issue.1 , pp. 97-102
    • Ranson, H.1    Prapanthadara, L.A.2    Hemingway, J.3
  • 37
    • 0025993434 scopus 로고
    • Purified glutathione S-transferase from parasites as candidate protective antigens
    • Sharp P.J., Smith D.R.J., Bach W., Wagland B.M., and Cobon G.S. Purified glutathione S-transferase from parasites as candidate protective antigens. Int. J. Parasitol. 21 (1991) 839-846
    • (1991) Int. J. Parasitol. , vol.21 , pp. 839-846
    • Sharp, P.J.1    Smith, D.R.J.2    Bach, W.3    Wagland, B.M.4    Cobon, G.S.5
  • 38
    • 0034728774 scopus 로고    scopus 로고
    • Tyrosine 50 at the subunit interface of dimeric human glutathione transferase P1-1 is a structural key residue for modulating protein stability and catalytic function
    • Stenberg G., Abdallah A.M., and Mannervik B. Tyrosine 50 at the subunit interface of dimeric human glutathione transferase P1-1 is a structural key residue for modulating protein stability and catalytic function. Biochem. Biophys. Res. Commun. 271 1 (2000) 59-63
    • (2000) Biochem. Biophys. Res. Commun. , vol.271 , Issue.1 , pp. 59-63
    • Stenberg, G.1    Abdallah, A.M.2    Mannervik, B.3
  • 39
    • 0028316477 scopus 로고
    • Inter-individual variability of human hepatic glutathione S-transferase isozymes assessed by inhibitory capacity
    • Takamatsu Y., and Inaba T. Inter-individual variability of human hepatic glutathione S-transferase isozymes assessed by inhibitory capacity. Toxicology 88 1-3 (1994) 191-200
    • (1994) Toxicology , vol.88 , Issue.1-3 , pp. 191-200
    • Takamatsu, Y.1    Inaba, T.2
  • 40
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76 (1979) 4350-4354
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 42
    • 0141889793 scopus 로고    scopus 로고
    • Purification, biochemical characterization, and cDNA cloning of a glutathione S-transferase from the red imported fire ant, Solenopsis invicta
    • Valles S.M., Perera O.P., and Strong C.A. Purification, biochemical characterization, and cDNA cloning of a glutathione S-transferase from the red imported fire ant, Solenopsis invicta. Insect Biochem. Mol. Biol. 33 10 (2003) 981-988
    • (2003) Insect Biochem. Mol. Biol. , vol.33 , Issue.10 , pp. 981-988
    • Valles, S.M.1    Perera, O.P.2    Strong, C.A.3
  • 43
    • 0141568868 scopus 로고    scopus 로고
    • Multiple roles of glutathione binding-site residues of glutathione S-transferase
    • Vararattanavech A., and Ketterman A.J. Multiple roles of glutathione binding-site residues of glutathione S-transferase. Protein Pept. Lett. 10 5 (2003) 441-448
    • (2003) Protein Pept. Lett. , vol.10 , Issue.5 , pp. 441-448
    • Vararattanavech, A.1    Ketterman, A.J.2
  • 44
    • 0035499462 scopus 로고    scopus 로고
    • Identification and cloning of a key insecticide-metabolizing glutathione S-transferase (MdGST-6A) from a hyper insecticide-resistant strain of the housefly Musca domestica
    • Wei S.H., Clark A.G., and Syvanen M. Identification and cloning of a key insecticide-metabolizing glutathione S-transferase (MdGST-6A) from a hyper insecticide-resistant strain of the housefly Musca domestica. Insect Biochem. Mol. Biol. 31 12 (2001) 1145-1153
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , Issue.12 , pp. 1145-1153
    • Wei, S.H.1    Clark, A.G.2    Syvanen, M.3
  • 45
    • 0025999878 scopus 로고
    • Cysteine residues are not essential for the catalytic activity of human class Mu glutathione transferase M1a-1a
    • Widersten M., Holmstrom E., and Mannervik B. Cysteine residues are not essential for the catalytic activity of human class Mu glutathione transferase M1a-1a. FEBS Lett. 293 1/2 (1991) 156-159
    • (1991) FEBS Lett. , vol.293 , Issue.1-2 , pp. 156-159
    • Widersten, M.1    Holmstrom, E.2    Mannervik, B.3
  • 46
    • 4544350247 scopus 로고    scopus 로고
    • Catalytic and structural contributions for glutathione-binding residues in a Delta class glutathione S-tranferases
    • Winayanuwattikun P., and Ketterman A.J. Catalytic and structural contributions for glutathione-binding residues in a Delta class glutathione S-tranferases. Biochem. J. 382 2 (2004) 751-757
    • (2004) Biochem. J. , vol.382 , Issue.2 , pp. 751-757
    • Winayanuwattikun, P.1    Ketterman, A.J.2
  • 47
    • 0021114956 scopus 로고
    • A set of inhibitors for discrimination between the basic isoenzymes of glutathione transferase in rat liver
    • Yalcin S., Jennsson H., and Mannervik B. A set of inhibitors for discrimination between the basic isoenzymes of glutathione transferase in rat liver. Biochem. Biophys. Res. Commun. 114 (1983) 829-834
    • (1983) Biochem. Biophys. Res. Commun. , vol.114 , pp. 829-834
    • Yalcin, S.1    Jennsson, H.2    Mannervik, B.3
  • 48
    • 0034086735 scopus 로고    scopus 로고
    • Purification and characterization of glutathione S-transferases from the German cockroach, Blattella germanica (L.)
    • Yu S.J., and Huang S.W. Purification and characterization of glutathione S-transferases from the German cockroach, Blattella germanica (L.). Pestic. Biochem. Physiol. 67 (2000) 36-45
    • (2000) Pestic. Biochem. Physiol. , vol.67 , pp. 36-45
    • Yu, S.J.1    Huang, S.W.2


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