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Volumn 93, Issue 5, 2006, Pages 1017-1022

High yield production of a mutant Nippostrongylus brasiliensis acetylcholinesterase in Pichia pastoris and its purification

Author keywords

Acetylcholinesterase; Biosensor; Fermentation; Nippostrongylus brasiliensis; Pichia pastoris; Purification

Indexed keywords

CELL CULTURE; CELLS; OXYGEN; PURIFICATION; YEAST;

EID: 33646056991     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.20705     Document Type: Article
Times cited : (22)

References (33)
  • 1
    • 0002630825 scopus 로고
    • Enzymatic destruction of acetylcholine
    • Hubbard JI, ed. New York: Plenum Press
    • Barnard EA. 1974. Enzymatic destruction of acetylcholine. In: Hubbard JI, ed. Peripheral Nervous System. New York: Plenum Press. p. 201-224.
    • (1974) Peripheral Nervous System , pp. 201-224
    • Barnard, E.A.1
  • 2
    • 0017184389 scopus 로고
    • A rapid method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analyt Biochem 72:248-254.
    • (1976) Analyt Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
  • 4
    • 0002283070 scopus 로고    scopus 로고
    • Expression in the methylotrophic yeast Pichia pastoris
    • Fernandez JM, Hofftler JP, editors. San Diego: Academic Press
    • Cregg JM. 1999. Expression in the methylotrophic yeast Pichia pastoris. In: Fernandez JM, Hofftler JP, editors. Gene expression systems-using nature for the art of expression. San Diego: Academic Press. pp 157-191.
    • (1999) Gene Expression Systems - Using Nature for the Art of Expression , pp. 157-191
    • Cregg, J.M.1
  • 7
    • 0032030173 scopus 로고    scopus 로고
    • Stabilisation of recombinant Drosophila acetylcholinesterase
    • Estrada-Mondaca S, Fournier D. 1998. Stabilisation of recombinant Drosophila acetylcholinesterase. Protein Expr Purification 12:166.
    • (1998) Protein Expr Purification , vol.12 , pp. 166
    • Estrada-Mondaca, S.1    Fournier, D.2
  • 9
    • 0032513163 scopus 로고    scopus 로고
    • Functional expression of a mammalian acetylcholinesterase in Pichia pastoris: Comparison to acetylcholinesterase, expressed and reconstituted from Escherichia coli
    • Heim J, Schmidt-Danert C, Atomi H, Schmid RD. 1998. Functional expression of a mammalian acetylcholinesterase in Pichia pastoris: Comparison to acetylcholinesterase, expressed and reconstituted from Escherichia coli. Biochim Biophys Acta 1396:306-319.
    • (1998) Biochim Biophys Acta , vol.1396 , pp. 306-319
    • Heim, J.1    Schmidt-Danert, C.2    Atomi, H.3    Schmid, R.D.4
  • 11
    • 0033515474 scopus 로고    scopus 로고
    • Cloning, expression and properties of a nonneuronal secreted acetylcholinesterase from the parasitic nematode Nippostrongylus brasiliensis
    • Hussein AS, Chacon MR, Smith AM, Tosado-Acevedo R, Selkirk ME. 1999. Cloning, expression and properties of a nonneuronal secreted acetylcholinesterase from the parasitic nematode Nippostrongylus brasiliensis. J Biol Chem 274:9312-9319.
    • (1999) J Biol Chem , vol.274 , pp. 9312-9319
    • Hussein, A.S.1    Chacon, M.R.2    Smith, A.M.3    Tosado-Acevedo, R.4    Selkirk, M.E.5
  • 12
    • 0034008857 scopus 로고    scopus 로고
    • Determinants of substrate specificity of a second non-neuronal secreted acetylcholinesterase from the parasitic nematode Nippostrongylus brasiliensis
    • Hussein AS, Smith AM, Chacon MR, Selkirk ME. 2000. Determinants of substrate specificity of a second non-neuronal secreted acetylcholinesterase from the parasitic nematode Nippostrongylus brasiliensis. Eur J Biochem 267:2276-2282.
    • (2000) Eur J Biochem , vol.267 , pp. 2276-2282
    • Hussein, A.S.1    Smith, A.M.2    Chacon, M.R.3    Selkirk, M.E.4
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • Lin Cereghino J, Cregg JM. 2001. Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol Rev 24:45-66.
    • (2001) FEMS Microbiol Rev , vol.24 , pp. 45-66
    • Lin Cereghino, J.1    Cregg, J.M.2
  • 15
    • 0017089228 scopus 로고
    • Affinity chromatography of acetylcholinesterase. The importance of hydrophobic interactions
    • Massoulie J, Bon S. 1976. Affinity chromatography of acetylcholinesterase. The importance of hydrophobic interactions. Eur J Biochem 68:531-539.
    • (1976) Eur J Biochem , vol.68 , pp. 531-539
    • Massoulie, J.1    Bon, S.2
  • 16
    • 0030696109 scopus 로고    scopus 로고
    • Expression and processing of vertebrate acetylcholinesterase in the yeast Pichia pastoris
    • Morel N, Massoulie J. 1997. Expression and processing of vertebrate acetylcholinesterase in the yeast Pichia pastoris. Biochem J 328:121-129.
    • (1997) Biochem J , vol.328 , pp. 121-129
    • Morel, N.1    Massoulie, J.2
  • 17
    • 0027978867 scopus 로고
    • Molecular recognition in acetylcholinesterase catalysis: Free-energy correlations for substrate turnover and inhibition by trifluoro ketone transition-state analogs
    • Nair HK, Seravalli J, Arbuckle T, Quinn DM. 1994. Molecular recognition in acetylcholinesterase catalysis: Free-energy correlations for substrate turnover and inhibition by trifluoro ketone transition-state analogs. Biochemistry 33:8566-8576.
    • (1994) Biochemistry , vol.33 , pp. 8566-8576
    • Nair, H.K.1    Seravalli, J.2    Arbuckle, T.3    Quinn, D.M.4
  • 18
    • 0020581758 scopus 로고
    • Use of procainamide gels in the purification of human and horse serum cholinesterase
    • Ralston JS, Main AR, Kilpatrick BF, Chasson AL. 1983. Use of procainamide gels in the purification of human and horse serum cholinesterase. Biochem J 211:243-250.
    • (1983) Biochem J , vol.211 , pp. 243-250
    • Ralston, J.S.1    Main, A.R.2    Kilpatrick, B.F.3    Chasson, A.L.4
  • 19
    • 0001704141 scopus 로고    scopus 로고
    • Synaptic transmission
    • Riddle DLT, Blumenthal TBJ, Meyer BJ, Priess JR, editors. Cold Spring Harbor, New York, USA: Cold Spring Harbor Laboratory Press
    • Rand JB, Nonet ML. 1997. Synaptic transmission. In: Riddle DLT, Blumenthal TBJ, Meyer BJ, Priess JR, editors. C. elegans II. Cold Spring Harbor, New York, USA: Cold Spring Harbor Laboratory Press. pp 611-643.
    • (1997) C. elegans II , pp. 611-643
    • Rand, J.B.1    Nonet, M.L.2
  • 20
    • 0021338810 scopus 로고
    • Structure of human erythrocyte acetylcholinesterase
    • Rosenberry TL, Scoggin DM. 1984. Structure of human erythrocyte acetylcholinesterase. J Biol Chem 259:5643-5652.
    • (1984) J Biol Chem , vol.259 , pp. 5643-5652
    • Rosenberry, T.L.1    Scoggin, D.M.2
  • 21
    • 0036883617 scopus 로고    scopus 로고
    • Development, validation, and application of an acetylcholinesterase- biosensor test for the direct detection of insecticide residues in infant food
    • Schulze H, Scherbaum E, Anastassiades M, Vorlova S, Schmid RD, Bachmann TT. 2002. Development, validation, and application of an acetylcholinesterase- biosensor test for the direct detection of insecticide residues in infant food. Biosens Bioelectron 17:1095-1105.
    • (2002) Biosens Bioelectron , vol.17 , pp. 1095-1105
    • Schulze, H.1    Scherbaum, E.2    Anastassiades, M.3    Vorlova, S.4    Schmid, R.D.5    Bachmann, T.T.6
  • 23
    • 1542617929 scopus 로고    scopus 로고
    • Activation of phosphorothionate pesticides based on a cytochrome P450 BM-3 (CYP 102 A1) mutant for expanded neurotoxin detection in food using acetylcholinesterase biosensors
    • Schulze H, Schmid RD, Bachmann TT. 2004. Activation of phosphorothionate pesticides based on a cytochrome P450 BM-3 (CYP 102 A1) mutant for expanded neurotoxin detection in food using acetylcholinesterase biosensors. Analyt Chem 76:1720-1725.
    • (2004) Analyt Chem , vol.76 , pp. 1720-1725
    • Schulze, H.1    Schmid, R.D.2    Bachmann, T.T.3
  • 24
    • 24944508568 scopus 로고    scopus 로고
    • Insecticide detection through protein engineering of Nippostrongylus brasiliensis acetylcholinesterase B
    • Schulze H, Muench SB, Villatte F, Schmid RD, Bachmann TT. 2005. Insecticide detection through protein engineering of Nippostrongylus brasiliensis acetylcholinesterase B. Analyt Chem 77:5823-5830.
    • (2005) Analyt Chem , vol.77 , pp. 5823-5830
    • Schulze, H.1    Muench, S.B.2    Villatte, F.3    Schmid, R.D.4    Bachmann, T.T.5
  • 25
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M. 1996. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Analyt Chem 68:850-858.
    • (1996) Analyt Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 28
    • 0024279312 scopus 로고
    • Purification and crystallization of a dimeric form of acetylcholinesterase from Torpedo californica subsequent to solubilization with phosphatidylinositol-specific phospholipase C
    • Sussman JL, Harel M, Frolow F, Varon L, Toker L, Futerman AH, Silman I. 1988. Purification and crystallization of a dimeric form of acetylcholinesterase from Torpedo californica subsequent to solubilization with phosphatidylinositol-specific phospholipase C. J Mol Biol 203:821-823.
    • (1988) J Mol Biol , vol.203 , pp. 821-823
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Varon, L.4    Toker, L.5    Futerman, A.H.6    Silman, I.7
  • 29
    • 0032052515 scopus 로고    scopus 로고
    • Cloning of clustered Streptomyces viridosporus T7A lignocellulose catabolism genes encoding peroxidase and endoglucanase and their extracellular expression in Pichia pastoris
    • Thomas L, Crawford DL. 1998. Cloning of clustered Streptomyces viridosporus T7A lignocellulose catabolism genes encoding peroxidase and endoglucanase and their extracellular expression in Pichia pastoris. Can J Microbiol 44:364-372.
    • (1998) Can J Microbiol , vol.44 , pp. 364-372
    • Thomas, L.1    Crawford, D.L.2
  • 30
    • 0032007153 scopus 로고    scopus 로고
    • Engineering sensitive acetylcholinesterase for detection of organophosphate and carbamate insecticides
    • Villatte F, Marcel V, Estrada-Mondaca S, Fournier D. 1998. Engineering sensitive acetylcholinesterase for detection of organophosphate and carbamate insecticides. Biosens Bioelectron 13:157-164.
    • (1998) Biosens Bioelectron , vol.13 , pp. 157-164
    • Villatte, F.1    Marcel, V.2    Estrada-Mondaca, S.3    Fournier, D.4
  • 31
    • 0033924767 scopus 로고    scopus 로고
    • A high number of mutations in insect acetylcholinesterase may provide insecticide resistance
    • Villatte F, Ziliani P, Marcel V, Menozzi P, Fournier D. 2000. A high number of mutations in insect acetylcholinesterase may provide insecticide resistance. Pesticide Biochem Physiol 67:95-102.
    • (2000) Pesticide Biochem Physiol , vol.67 , pp. 95-102
    • Villatte, F.1    Ziliani, P.2    Marcel, V.3    Menozzi, P.4    Fournier, D.5
  • 33
    • 0032790856 scopus 로고    scopus 로고
    • High yield secretion of recombinant gelatins by Pichia pastoris
    • Werten M, van den Bosch T, Wind R, Mooi Broek H, de Wolf F. 1999. High yield secretion of recombinant gelatins by Pichia pastoris. Yeast 15(11):1087-1096.
    • (1999) Yeast , vol.15 , Issue.11 , pp. 1087-1096
    • Werten, M.1    Van Den Bosch, T.2    Wind, R.3    Mooi Broek, H.4    De Wolf, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.