메뉴 건너뛰기




Volumn 1, Issue 2, 2006, Pages 1006-1021

Production of recombinant protein in Pichia pastoris by fermentation

Author keywords

[No Author keywords available]

Indexed keywords

RECOMBINANT PROTEIN;

EID: 33845593592     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2006.126     Document Type: Article
Times cited : (72)

References (28)
  • 2
    • 14744285206 scopus 로고    scopus 로고
    • Expression of heterologous proteins in Pichia pastoris: A useful experimental tool in protein engineering and production
    • Daly, R. & Hearn, M.T. Expression of heterologous proteins in Pichia pastoris: A useful experimental tool in protein engineering and production. J. Mol. Recognit. 18, 119-138 (2005).
    • (2005) J. Mol. Recognit , vol.18 , pp. 119-138
    • Daly, R.1    Hearn, M.T.2
  • 3
    • 17244363998 scopus 로고    scopus 로고
    • Heterologous protein production using the Pichia pastoris expression system
    • Macauley-Patrick, S., Fazenda, M.L., McNeil, B. & Harvey, L.M. Heterologous protein production using the Pichia pastoris expression system. Yeast 22, 249-270 (2005).
    • (2005) Yeast , vol.22 , pp. 249-270
    • Macauley-Patrick, S.1    Fazenda, M.L.2    McNeil, B.3    Harvey, L.M.4
  • 4
    • 29544447324 scopus 로고    scopus 로고
    • Recombinant microbial systems for the production of human collagen and gelatin
    • Baez, J., Olsen, D. & Polarek, J.W. Recombinant microbial systems for the production of human collagen and gelatin. Appl. Microbiol. Biotechnol. 69, 245-252 (2005).
    • (2005) Appl. Microbiol. Biotechnol , vol.69 , pp. 245-252
    • Baez, J.1    Olsen, D.2    Polarek, J.W.3
  • 5
    • 0034610097 scopus 로고    scopus 로고
    • Modeling Pichia pastoris growth on methanol and optimizing the production of a recombinant protein, the heavy-chain fragment C of botulinum neurotoxin, serotype A
    • Zhang, W., Bevins, M.A., Plantz, B.A., Smith, L.A. & Meagher, M.M. Modeling Pichia pastoris growth on methanol and optimizing the production of a recombinant protein, the heavy-chain fragment C of botulinum neurotoxin, serotype A. Biotechnol. Bioeng. 70, 1-8 (2000).
    • (2000) Biotechnol. Bioeng , vol.70 , pp. 1-8
    • Zhang, W.1    Bevins, M.A.2    Plantz, B.A.3    Smith, L.A.4    Meagher, M.M.5
  • 8
    • 85131322392 scopus 로고    scopus 로고
    • Deglycosylation to obtain stable and homogeneous Pichia pastoris-expressed N-A1 domains of carcinoembryonic antigen
    • in press
    • Sainz-Pastor, N. et al. Deglycosylation to obtain stable and homogeneous Pichia pastoris-expressed N-A1 domains of carcinoembryonic antigen. Int. J. Biol. Macromol. (in press)
    • Int. J. Biol. Macromol
    • Sainz-Pastor, N.1
  • 9
    • 19944427731 scopus 로고    scopus 로고
    • Sustained tumor regression of human colorectal cancer xenografts using a multifunctional mannosylated fusion protein in antibody-directed enzyme prodrug therapy
    • Sharma, S.K. et al. Sustained tumor regression of human colorectal cancer xenografts using a multifunctional mannosylated fusion protein in antibody-directed enzyme prodrug therapy. Clin. Cancer Res. 11 814-825 (2005).
    • (2005) Clin. Cancer Res , vol.11 , pp. 814-825
    • Sharma, S.K.1
  • 10
    • 3943101478 scopus 로고    scopus 로고
    • Radiolabelling of glycosylated MFE-23::CPG2 fusion protein (MFECP1) with Tc-99m for quantitation of tumour antibody-enzyme localisation in antibody-directed enzyme pro-drug therapy (ADEPT)
    • Francis, R.J. et al. Radiolabelling of glycosylated MFE-23::CPG2 fusion protein (MFECP1) with Tc-99m for quantitation of tumour antibody-enzyme localisation in antibody-directed enzyme pro-drug therapy (ADEPT). European J. Nuclear Med. Mol. Imaging 31, 1090-1096 (2004).
    • (2004) European J. Nuclear Med. Mol. Imaging , vol.31 , pp. 1090-1096
    • Francis, R.J.1
  • 11
    • 34548816805 scopus 로고    scopus 로고
    • A phase I study of single administration of antibody-directed enzyme prodrug therapy (ADEPT) with the recombinant anti-CEA antibody-enzyme fusion protein MFECP1 and a bis-iodo phenol mustard prodrug
    • Mayer, A. et al. A phase I study of single administration of antibody-directed enzyme prodrug therapy (ADEPT) with the recombinant anti-CEA antibody-enzyme fusion protein MFECP1 and a bis-iodo phenol mustard prodrug. Clin. Cancer Res. (in press).
    • Clin. Cancer Res. (in press)
    • Mayer, A.1
  • 12
    • 0033983443 scopus 로고    scopus 로고
    • Catalytic activity of an in vivo tumor targeted anti-CEA scFv::Carboxypeptidase G2 fusion protein
    • Bhatia, J. et al. Catalytic activity of an in vivo tumor targeted anti-CEA scFv::Carboxypeptidase G2 fusion protein. Int. J. Cancer 85, 571-577 (2000).
    • (2000) Int. J. Cancer , vol.85 , pp. 571-577
    • Bhatia, J.1
  • 14
    • 0026327987 scopus 로고
    • Structure of oligosaccharides on Saccharomyces SUC2 invertase secreted by the methylotrophic yeast
    • Trimble, R.B., Atkinson, P.H., Tschopp, J.F., Townsend, R.R. & Maley, F. Structure of oligosaccharides on Saccharomyces SUC2 invertase secreted by the methylotrophic yeast. Pichia pastoris. J. Biol. Chem. 266, 22807-22817 (1991).
    • (1991) Pichia pastoris. J. Biol. Chem , vol.266 , pp. 22807-22817
    • Trimble, R.B.1    Atkinson, P.H.2    Tschopp, J.F.3    Townsend, R.R.4    Maley, F.5
  • 15
    • 0742324507 scopus 로고    scopus 로고
    • Glycoforms obtained by expression in Pichia pastoris improve cancer targeting potential of a recombinant antibody-enzyme fusion protein
    • Medzihradszky, K. F. et al. Glycoforms obtained by expression in Pichia pastoris improve cancer targeting potential of a recombinant antibody-enzyme fusion protein. Glycobiology 14, 27-37 (2004).
    • (2004) Glycobiology , vol.14 , pp. 27-37
    • Medzihradszky, K.F.1
  • 16
    • 8344271025 scopus 로고    scopus 로고
    • Advances in the production of human therapeutic proteins in yeasts and filamentous fungi
    • Gemgross, T.U. Advances in the production of human therapeutic proteins in yeasts and filamentous fungi. Nat. Biotechnol. 22, 1409-1414 (2004).
    • (2004) Nat. Biotechnol , vol.22 , pp. 1409-1414
    • Gemgross, T.U.1
  • 17
    • 21144469605 scopus 로고    scopus 로고
    • Phase 1 clinical trial of apical membrane antigen 1: An asexual blood-stage vaccine for Plasmodium falciparum malaria
    • Malkin, E.M. et al. Phase 1 clinical trial of apical membrane antigen 1: An asexual blood-stage vaccine for Plasmodium falciparum malaria. Infect. Immun. 73, 3677-3685 (2005).
    • (2005) Infect. Immun , vol.73 , pp. 3677-3685
    • Malkin, E.M.1
  • 18
    • 0037106261 scopus 로고    scopus 로고
    • Phase I study of recombinant human endostatin in patients with advanced solid tumors
    • Herbst, R.S. et al. Phase I study of recombinant human endostatin in patients with advanced solid tumors. J. Clin. Oncol. 20, 3792-3803 (2002).
    • (2002) J. Clin. Oncol , vol.20 , pp. 3792-3803
    • Herbst, R.S.1
  • 19
    • 33644500755 scopus 로고    scopus 로고
    • Summary of recombinant human serum albumin development
    • Kobayashi, K. Summary of recombinant human serum albumin development. Biologicals 34, 55-59 (2006).
    • (2006) Biologicals , vol.34 , pp. 55-59
    • Kobayashi, K.1
  • 20
    • 32344449790 scopus 로고    scopus 로고
    • Optimization of humanized IgGs in glycoengineered Pichia pastoris
    • Li, H. et al. Optimization of humanized IgGs in glycoengineered Pichia pastoris. Nat. Biotechnol. 24, 210-215 (2006).
    • (2006) Nat. Biotechnol , vol.24 , pp. 210-215
    • Li, H.1
  • 21
    • 0037430841 scopus 로고    scopus 로고
    • Analysis and control of proteolysis of a fusion protein in Pichia pastoris fed-batch processes
    • Jahic, M., Gustavsson, M., Jansen, A.K., Martinelle, M. & Enfors, S.O. Analysis and control of proteolysis of a fusion protein in Pichia pastoris fed-batch processes. J. Biotechnol. 102, 45-53 (2003).
    • (2003) J. Biotechnol , vol.102 , pp. 45-53
    • Jahic, M.1    Gustavsson, M.2    Jansen, A.K.3    Martinelle, M.4    Enfors, S.O.5
  • 22
    • 12144251696 scopus 로고    scopus 로고
    • Causes of proteolytic degradation of secreted recombinant proteins produced in methylotrophic yeast Pichia pastoris: Case study with recombinant ovine interferon-τ
    • Sinha, J., Plantz, B.A., Inan, M. & Meagher, M.M. Causes of proteolytic degradation of secreted recombinant proteins produced in methylotrophic yeast Pichia pastoris: Case study with recombinant ovine interferon-τ. Biotechnol. Bioeng. 89, 102-112 (2005).
    • (2005) Biotechnol. Bioeng , vol.89 , pp. 102-112
    • Sinha, J.1    Plantz, B.A.2    Inan, M.3    Meagher, M.M.4
  • 23
    • 0033975293 scopus 로고    scopus 로고
    • High-level expression of recombinant human serum albumin from the methylotrophic yeast Pichia pastoris with minimal protease production and activation
    • Kobayashi, K. et al. High-level expression of recombinant human serum albumin from the methylotrophic yeast Pichia pastoris with minimal protease production and activation. J. Biosci. Bioeng. 89, 55-61 (2000).
    • (2000) J. Biosci. Bioeng , vol.89 , pp. 55-61
    • Kobayashi, K.1
  • 24
    • 19944417953 scopus 로고    scopus 로고
    • Improved yield of recombinant merozoite surface protein 3 (MSP3) from Pichia pastoris using chemically defined media
    • Wang, J. et al. Improved yield of recombinant merozoite surface protein 3 (MSP3) from Pichia pastoris using chemically defined media. Biotechnol. Bioeng. 90, 838-847 (2005).
    • (2005) Biotechnol. Bioeng , vol.90 , pp. 838-847
    • Wang, J.1
  • 25
    • 0032790856 scopus 로고    scopus 로고
    • High-yield secretion of recombinant gelatins by Pichia pastoris
    • Werten, M.W. et al. High-yield secretion of recombinant gelatins by Pichia pastoris. Yeast 15, 1087-1096 (1999).
    • (1999) Yeast , vol.15 , pp. 1087-1096
    • Werten, M.W.1
  • 26
    • 0035715001 scopus 로고    scopus 로고
    • Low-temperature increases the yield of biologically active herring antifreeze protein in Pichia pastoris
    • Li, Z.J. et al. Low-temperature increases the yield of biologically active herring antifreeze protein in Pichia pastoris. Protein Expr. Purif. 21, 438-445 (2001).
    • (2001) Protein Expr. Purif , vol.21 , pp. 438-445
    • Li, Z.J.1
  • 27
    • 2442661971 scopus 로고    scopus 로고
    • In vivo synthesis of mammalian-like, hybrid-type N-glycans in Pichia pastoris
    • Vervecken, W. et al. In vivo synthesis of mammalian-like, hybrid-type N-glycans in Pichia pastoris. Appl. Environ. Microbiol. 70, 2639-2646 (2004).
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 2639-2646
    • Vervecken, W.1
  • 28
    • 8844263095 scopus 로고    scopus 로고
    • Identification and removal of O-linked and non-covalently linked sugars from recombinant protein produced using Pichia pastoris
    • O'Leary, J.M. et al. Identification and removal of O-linked and non-covalently linked sugars from recombinant protein produced using Pichia pastoris. Protein Expr. Purif. 38, 217-227 (2004).
    • (2004) Protein Expr. Purif , vol.38 , pp. 217-227
    • O'Leary, J.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.