메뉴 건너뛰기




Volumn 27, Issue 2, 2003, Pages 229-237

Methylotrophic yeast Pichia pastoris as a host for production of ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum)

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL OXIDOREDUCTASES; APYRASE; BASE SEQUENCE; BLOTTING, WESTERN; CATIONS; CHROMATOGRAPHY, ION EXCHANGE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GENETIC VECTORS; GLYCOSYLATION; METHANOL; MODELS, CHEMICAL; MODELS, GENETIC; MOLECULAR SEQUENCE DATA; MUTAGENESIS; OLIGONUCLEOTIDES; PHOSPHATES; PICHIA; PLASMIDS; PROMOTER REGIONS (GENETICS); RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SEQUENCE ANALYSIS, DNA; SOLANUM;

EID: 0037296231     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1046-5928(02)00605-8     Document Type: Article
Times cited : (22)

References (41)
  • 2
    • 0030064372 scopus 로고    scopus 로고
    • Apyrases (ATP diphosphohydrolases, EC 3.6.1.5): Function and relationship to ATPases
    • M. Komoszynski, A. Wojtczak, Apyrases (ATP diphosphohydrolases, EC 3.6.1.5): function and relationship to ATPases, Biochim. Biophys. Acta 1310 (1996) 233-241.
    • (1996) Biochim. Biophys. Acta , vol.1310 , pp. 233-241
    • Komoszynski, M.1    Wojtczak, A.2
  • 3
    • 0030034867 scopus 로고    scopus 로고
    • Purification and cloning of a soluble ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum)
    • M. Handa, G. Guidotti, Purification and cloning of a soluble ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum), Biochem. Biophys. Res. Commun. 218 (1996) 916-923.
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 916-923
    • Handa, M.1    Guidotti, G.2
  • 4
    • 0028967657 scopus 로고
    • Ecto-ATPases: Identities and functions
    • L. Plesner, Ecto-ATPases: identities and functions, Int. Rev. Cytol. 158 (1995) 141-214.
    • (1995) Int. Rev. Cytol. , vol.158 , pp. 141-214
    • Plesner, L.1
  • 5
    • 0028041238 scopus 로고
    • Signalling via ATP in the nervous system
    • H. Zimmermann, Signalling via ATP in the nervous system, Trends Neurosci. 17 (1994) 420-426.
    • (1994) Trends Neurosci. , vol.17 , pp. 420-426
    • Zimmermann, H.1
  • 9
    • 0027327079 scopus 로고
    • Guanosine diphosphatase is required for protein and sphingolipid glycosylation in the Golgi lumen of Saccharomyces cerevisiae
    • C. Abeijon, K. Yanagisawa, E.C. Mandon, A. Hausler, K. Moremen, C.B. Hirschberg, P.W. Robbins, Guanosine diphosphatase is required for protein and sphingolipid glycosylation in the Golgi lumen of Saccharomyces cerevisiae, J. Cell Biol. 122 (1993) 307-323.
    • (1993) J. Cell Biol. , vol.122 , pp. 307-323
    • Abeijon, C.1    Yanagisawa, K.2    Mandon, E.C.3    Hausler, A.4    Moremen, K.5    Hirschberg, C.B.6    Robbins, P.W.7
  • 10
    • 0027416764 scopus 로고
    • Epidermal Langerhans cells are resistant to the permeabilizing effects of extracellular ATP: In vitro evidence supporting a protective role of membrane ATPase
    • G. Girolomoni, M.L. Santantonio, S. Pastore, P.R. Bergstresser, A. Giannetti, P.D. Cruz Jr., Epidermal Langerhans cells are resistant to the permeabilizing effects of extracellular ATP: in vitro evidence supporting a protective role of membrane ATPase, J. Invest. Dermatol. 100 (1993) 282-287.
    • (1993) J. Invest. Dermatol. , vol.100 , pp. 282-287
    • Girolomoni, G.1    Santantonio, M.L.2    Pastore, S.3    Bergstresser, P.R.4    Giannetti, A.5    Cruz, P.D.6
  • 12
    • 0024387006 scopus 로고
    • Localization of the ecto-ATPase (ecto-nucleotidase) in the rat hepatocyte plasma membrane. Implications for the functions of the ecto-ATPase
    • S.H. Lin, Localization of the ecto-ATPase (ecto-nucleotidase) in the rat hepatocyte plasma membrane. Implications for the functions of the ecto-ATPase, J. Biol. Chem. 264 (1989) 14403-14407.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14403-14407
    • Lin, S.H.1
  • 13
    • 0026764064 scopus 로고
    • Mg(2+)-ATPase from rabbit skeletal muscle transverse tubules is 67-kilodalton glycoprotein
    • M.J. Treuheit, P.L. Vaghy, T.L. Kirley, Mg(2+)-ATPase from rabbit skeletal muscle transverse tubules is 67-kilodalton glycoprotein, J. Biol. Chem. 267 (1992) 11777-11782.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11777-11782
    • Treuheit, M.J.1    Vaghy, P.L.2    Kirley, T.L.3
  • 14
    • 0028109187 scopus 로고
    • Purification and characterization of the ecto-Mg-ATPase of chicken gizzard smooth muscle
    • J.G. Stout, T.L. Kirley, Purification and characterization of the ecto-Mg-ATPase of chicken gizzard smooth muscle, J. Biochem. Biophys. Methods 29 (1994) 61-75.
    • (1994) J. Biochem. Biophys. Methods , vol.29 , pp. 61-75
    • Stout, J.G.1    Kirley, T.L.2
  • 15
    • 0025718488 scopus 로고
    • ATP diphosphohydrolase is responsible for ecto-ATPase and ecto-ADPase activities in bovine aorta endothelial and smooth muscle cells
    • K. Yagi, M. Shinbo, M. Hashizume, L.S. Shimba, S. Kurimura, Y. Miura, ATP diphosphohydrolase is responsible for ecto-ATPase and ecto-ADPase activities in bovine aorta endothelial and smooth muscle cells, Biochem. Biophys. Res. Commun. 180 (1991) 1200-1206.
    • (1991) Biochem. Biophys. Res. Commun. , vol.180 , pp. 1200-1206
    • Yagi, K.1    Shinbo, M.2    Hashizume, M.3    Shimba, L.S.4    Kurimura, S.5    Miura, Y.6
  • 16
    • 0027412463 scopus 로고
    • Demonstration of a novel type of ATP-diphosphohydrolase (EC 3.6.1.5) in the bovine lung
    • M. Picher, Y.P. Cote, R. Beliveau, M. Potier, A.R. Beaudoin, Demonstration of a novel type of ATP-diphosphohydrolase (EC 3.6.1.5) in the bovine lung, J. Biol. Chem. 268 (1993) 4699-4703.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4699-4703
    • Picher, M.1    Cote, Y.P.2    Beliveau, R.3    Potier, M.4    Beaudoin, A.R.5
  • 17
    • 0028036717 scopus 로고
    • Tandemly repeated genes encode nucleoside triphosphate hydrolase isoforms secreted into the parasitophorous vacuole of Toxoplasma gondii
    • D. Bermudes, K.R. Peck, M.A. Afifi, C.J. Beckers, K.A. Joiner, Tandemly repeated genes encode nucleoside triphosphate hydrolase isoforms secreted into the parasitophorous vacuole of Toxoplasma gondii, J. Biol. Chem. 269 (1994) 29252-29260.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29252-29260
    • Bermudes, D.1    Peck, K.R.2    Afifi, M.A.3    Beckers, C.J.4    Joiner, K.A.5
  • 18
    • 0032722058 scopus 로고    scopus 로고
    • Golgi E-type ATPase with an unusual membrane topology
    • X. Zhong, G. Guidotti, A yeast Golgi E-type ATPase with an unusual membrane topology, J. Biol. Chem. 274 (1999) 32704-32711.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32704-32711
    • Zhong, X.1    Guidotti, G.2    Yeast, A.3
  • 20
    • 0033808460 scopus 로고    scopus 로고
    • Disaggregation of aggregated platelets by apyrase from the tick, Ornithodoros savignyi (Acari: Argasidae)
    • B.J. Mans, J. Coetzee, A.I. Louw, A.R. Gaspar, A.W. Neitz, Disaggregation of aggregated platelets by apyrase from the tick, Ornithodoros savignyi (Acari: Argasidae), Exp. Appl. Acarol. 24 (2000) 271-282.
    • (2000) Exp. Appl. Acarol. , vol.24 , pp. 271-282
    • Mans, B.J.1    Coetzee, J.2    Louw, A.I.3    Gaspar, A.R.4    Neitz, A.W.5
  • 21
    • 0032956266 scopus 로고    scopus 로고
    • Most apyrase preparations are impure and contain inhibitors of cathepsin G: Suggestions for use of apyrase in preparation and stabilization of platelet suspensions
    • R.L. Kinlough-Rathbone, D.W. Perry, M.L. Rand, M.A. Packham, Most apyrase preparations are impure and contain inhibitors of cathepsin G: suggestions for use of apyrase in preparation and stabilization of platelet suspensions, Thromb. Haemost. 81 (1999) 849-850.
    • (1999) Thromb. Haemost. , vol.81 , pp. 849-850
    • Kinlough-Rathbone, R.L.1    Perry, D.W.2    Rand, M.L.3    Packham, M.A.4
  • 22
    • 0017046904 scopus 로고
    • A method for the removal of platelet aggregating activity of commercial apyrase
    • K.A. Whigham, A.H. Drummond, W. Edgar, C.R. Prentice, A method for the removal of platelet aggregating activity of commercial apyrase, Thromb. Haemost. 36 (1976) 652-653.
    • (1976) Thromb. Haemost. , vol.36 , pp. 652-653
    • Whigham, K.A.1    Drummond, A.H.2    Edgar, W.3    Prentice, C.R.4
  • 23
    • 0029416790 scopus 로고
    • Use of enzyme somase in the measurement of biofilm using bioluminoscence
    • M. Greetham, B. Holden, J. Scutt, Use of enzyme somase in the measurement of biofilm using bioluminoscence, Water Sci. Tech. 32 (1995) 221-225.
    • (1995) Water Sci. Tech. , vol.32 , pp. 221-225
    • Greetham, M.1    Holden, B.2    Scutt, J.3
  • 24
    • 0027951281 scopus 로고
    • Apyrase immobilized on paramagnetic beads used to improve detection limits in bioluminometric ATP monitoring
    • P. Nyrén, Apyrase immobilized on paramagnetic beads used to improve detection limits in bioluminometric ATP monitoring, J. Biolumin. Chemilumin. 9 (1994) 29-34.
    • (1994) J. Biolumin. Chemilumin. , vol.9 , pp. 29-34
    • Nyrén, P.1
  • 26
    • 0032540905 scopus 로고    scopus 로고
    • A sequencing method based on real-time pyrophosphate
    • M. Ronaghi, M. Uhlén, P. Nyrén, A sequencing method based on real-time pyrophosphate, Science 281 (1998) 363-365.
    • (1998) Science , vol.281 , pp. 363-365
    • Ronaghi, M.1    Uhlén, M.2    Nyrén, P.3
  • 27
    • 14744304041 scopus 로고
    • Rapid selection using G418 of high copy number transformants of Pichia pastoris for high-level foreign gene expression
    • C.A. Scorer, J.J. Clare, W.R. McCombie, M.A. Romanos, K. Sreekrishna, Rapid selection using G418 of high copy number transformants of Pichia pastoris for high-level foreign gene expression, Biotechnology (N. Y.) 12 (1994) 181-184.
    • (1994) Biotechnology (N. Y.) , vol.12 , pp. 181-184
    • Scorer, C.A.1    Clare, J.J.2    McCombie, W.R.3    Romanos, M.A.4    Sreekrishna, K.5
  • 29
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • S.N. Ho, H.D. Hunt, R.M. Horton, J.K. Pullen, L.R. Pease, Site-directed mutagenesis by overlap extension using the polymerase chain reaction, Gene 77 (1989) 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 31
    • 0034622620 scopus 로고    scopus 로고
    • Mutation detection by Pyrosequencing: Sequencing of exons 5 to 8 of the p53 tumor suppressor gene
    • C.A. Garcia, A. Ahmadian, B. Gharizadeh, J. Lundeberg, M. Ronaghi, P. Nyrén, Mutation detection by Pyrosequencing: sequencing of exons 5 to 8 of the p53 tumor suppressor gene, Gene 253 (2000) 249-257.
    • (2000) Gene , vol.253 , pp. 249-257
    • Garcia, C.A.1    Ahmadian, A.2    Gharizadeh, B.3    Lundeberg, J.4    Ronaghi, M.5    Nyrén, P.6
  • 33
    • 0030862156 scopus 로고    scopus 로고
    • Identification of residues essential for differential fatty acyl specificity of Geotrichum candidum lipases I and II
    • M. Holmquist, D.C. Tessier, M. Cygler, Identification of residues essential for differential fatty acyl specificity of Geotrichum candidum lipases I and II, Biochemistry 36 (1997) 15019-15025.
    • (1997) Biochemistry , vol.36 , pp. 15019-15025
    • Holmquist, M.1    Tessier, D.C.2    Cygler, M.3
  • 34
    • 0035715790 scopus 로고    scopus 로고
    • Expression in Pichia pastoris of Candida antarctica lipase B and lipase B fused to a cellulose-binding domain
    • J.C. Rotticci-Mulder, M. Gustavsson, M. Holmquist, K. Hult, M. Martinelle, Expression in Pichia pastoris of Candida antarctica lipase B and lipase B fused to a cellulose-binding domain, Protein Expr. Purif. 21 (2001) 386-392.
    • (2001) Protein Expr. Purif. , vol.21 , pp. 386-392
    • Rotticci-Mulder, J.C.1    Gustavsson, M.2    Holmquist, M.3    Hult, K.4    Martinelle, M.5
  • 35
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding
    • M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding, Anal. Biochem. 72 (1973) 248-254.
    • (1973) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 36
    • 0029115587 scopus 로고
    • Photometric microtiter assay of inorganic phosphate in the presence of acid-labile organic phosphates
    • P. Drueckes, R. Schinzel, D. Palm, Photometric microtiter assay of inorganic phosphate in the presence of acid-labile organic phosphates, Anal. Biochem. 230 (1995) 173-177.
    • (1995) Anal. Biochem. , vol.230 , pp. 173-177
    • Drueckes, P.1    Schinzel, R.2    Palm, D.3
  • 37
    • 0034891340 scopus 로고    scopus 로고
    • Bioluminometric method for realtime detection of ATPase activity
    • S. Karamohamed, G. Guidotti, Bioluminometric method for realtime detection of ATPase activity, Biotechniques 31 (2001) 420-425.
    • (2001) Biotechniques , vol.31 , pp. 420-425
    • Karamohamed, S.1    Guidotti, G.2
  • 39
    • 0000823705 scopus 로고
    • High level secretion of glycosylated invertase in the methylotropic yeast Pichia pastoris
    • J.F. Tshopp, G. Sverlow, C.W. Kosson, L. Grinna, High level secretion of glycosylated invertase in the methylotropic yeast Pichia pastoris, BioTechnology 5 (1987) 1305-1308.
    • (1987) BioTechnology , vol.5 , pp. 1305-1308
    • Tshopp, J.F.1    Sverlow, G.2    Kosson, C.W.3    Grinna, L.4
  • 40
    • 0031172410 scopus 로고    scopus 로고
    • Expression in Pichia pastoris and purification of Aspergillus awamori glucoamylase catalytic domain
    • H. Heimo, K. Palmu, I. Suominen, Expression in Pichia pastoris and purification of Aspergillus awamori glucoamylase catalytic domain, Protein Expr. Purif. 10 (1997) 70-79.
    • (1997) Protein Expr. Purif. , vol.10 , pp. 70-79
    • Heimo, H.1    Palmu, K.2    Suominen, I.3
  • 41
    • 0032006502 scopus 로고    scopus 로고
    • Human placental alkaline phosphatase: Expression in Pichia pastoris, purification and characterization of the enzyme
    • H. Heimo, K. Palmu, I. Suominen, Human placental alkaline phosphatase: expression in Pichia pastoris, purification and characterization of the enzyme, Protein Expr. Purif. 12 (1998) 85-92.
    • (1998) Protein Expr. Purif. , vol.12 , pp. 85-92
    • Heimo, H.1    Palmu, K.2    Suominen, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.