메뉴 건너뛰기




Volumn 35, Issue 2, 2004, Pages 284-292

Recombinant human serum amyloid P component from Pichia pastoris: Production and characterization

Author keywords

Pichia pastoris; Recombinant; Serum amyloid P component

Indexed keywords

INFLUENZA A VIRUS; INFLUENZA VIRUS; PICHIA; PICHIA PASTORIS; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 2642521353     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2004.01.011     Document Type: Article
Times cited : (8)

References (31)
  • 3
    • 0023617937 scopus 로고
    • Serum amyloid P component is the major calcium-dependent specific DNA binding protein of the serum
    • M.B. Pepys, P.J.G. Butler, Serum amyloid P component is the major calcium-dependent specific DNA binding protein of the serum, Biochem. Biophys. Res. Commun. 148 (1987) 308-313.
    • (1987) Biochem. Biophys. Res. Commun. , vol.148 , pp. 308-313
    • Pepys, M.B.1    Butler, P.J.G.2
  • 5
    • 0029010736 scopus 로고
    • Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimers disease and the systemic amyloidosis
    • G.A. Tennent, L.B. Lovat, M.B. Pepys, Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimers disease and the systemic amyloidosis, Proc. Nat. Acad. Sci. USA 92 (1995) 4299-4303.
    • (1995) Proc. Nat. Acad. Sci. USA , vol.92 , pp. 4299-4303
    • Tennent, G.A.1    Lovat, L.B.2    Pepys, M.B.3
  • 8
    • 0030769535 scopus 로고    scopus 로고
    • Serum amyloid P component binds to influenza A virus haemagglutinin and inhibits the virus infection in vitro
    • O. Andersen, K.V. Ravn, I. Juul Sørensen, G. Jonson, E. Holm Nielsen, S.-E. Svehag, Serum amyloid P component binds to influenza A virus haemagglutinin and inhibits the virus infection in vitro, Scand. J. Immunol. 46 (1997) 331-337.
    • (1997) Scand. J. Immunol. , vol.46 , pp. 331-337
    • Andersen, O.1    Ravn, K.V.2    Juul Sørensen, I.3    Jonson, G.4    Holm Nielsen, E.5    Svehag, S.-E.6
  • 11
    • 0002999388 scopus 로고
    • An improved galvanic cell for determination of oxygen concentration in fluids
    • F.J.H. Mackerth, An improved galvanic cell for determination of oxygen concentration in fluids, J. Sci. Instrum. 41 (1964) 38-41.
    • (1964) J. Sci. Instrum. , vol.41 , pp. 38-41
    • Mackerth, F.J.H.1
  • 12
    • 0028027806 scopus 로고
    • On-line growth measurements in bioreactors by titrating metabolic proton exchange
    • J.J.L. Iversen, J.K. Thomsen, R.P. Cox, On-line growth measurements in bioreactors by titrating metabolic proton exchange, Microbiol. Biotechnol. 42 (1994) 256-262.
    • (1994) Microbiol. Biotechnol. , vol.42 , pp. 256-262
    • Iversen, J.J.L.1    Thomsen, J.K.2    Cox, R.P.3
  • 13
    • 0035813451 scopus 로고    scopus 로고
    • Automatic inducer addition and harvesting of recombinant Escherichia coli cultures based on indirect on-line estimation of biomass concentration and specific growth rate
    • N.T. Eriksen, I. Kratchmarova, S. Neve, K. Kristiansen, J.J.L. Iversen, Automatic inducer addition and harvesting of recombinant Escherichia coli cultures based on indirect on-line estimation of biomass concentration and specific growth rate, Biotechnol. Bioeng. 75 (2001) 355-361.
    • (2001) Biotechnol. Bioeng. , vol.75 , pp. 355-361
    • Eriksen, N.T.1    Kratchmarova, I.2    Neve, S.3    Kristiansen, K.4    Iversen, J.J.L.5
  • 14
    • 0018720271 scopus 로고
    • A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels
    • R.C. Switser, C.R. Merril, S. Shifrin, A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels, Anal. Biochem. 98 (1979) 231-237.
    • (1979) Anal. Biochem. , vol.98 , pp. 231-237
    • Switser, R.C.1    Merril, C.R.2    Shifrin, S.3
  • 15
    • 0028185329 scopus 로고
    • Two-dimensional polyacrylamide gel electrophoresis using flat-bed isoelectric focusing in the first dimension
    • M.J. Dunn, Two-dimensional polyacrylamide gel electrophoresis using flat-bed isoelectric focusing in the first dimension, Methods Mol. Biol. 32 (1994) 227-232.
    • (1994) Methods Mol. Biol. , vol.32 , pp. 227-232
    • Dunn, M.J.1
  • 17
    • 0002572930 scopus 로고    scopus 로고
    • Ni-NTA for large-scale IMAC processes-systematic investigation of separation characteristics, storage and CIP conditions and leaching
    • F. Schäfer, J. Blümer, K. Steinert, Ni-NTA for large-scale IMAC processes-systematic investigation of separation characteristics, storage and CIP conditions and leaching, News Issue QIAGEN 4 (2000) 11-15.
    • (2000) News Issue QIAGEN , vol.4 , pp. 11-15
    • Schäfer, F.1    Blümer, J.2    Steinert, K.3
  • 18
    • 0035118541 scopus 로고    scopus 로고
    • Characterization of toxoplasma gondii surface antigen 1 (SAG1) secreted from Pichia pastoris: Evidence of hyper O-glycosylation
    • O. Letourneur, G. Gervasi, S. Gaja, J. Pagés, B. Watelet, M. Jolivet, Characterization of toxoplasma gondii surface antigen 1 (SAG1) secreted from Pichia pastoris: evidence of hyper O-glycosylation, Biotechnol. Appl. Biochem. 33 (2001) 35-45.
    • (2001) Biotechnol. Appl. Biochem. , vol.33 , pp. 35-45
    • Letourneur, O.1    Gervasi, G.2    Gaja, S.3    Pagés, J.4    Watelet, B.5    Jolivet, M.6
  • 19
    • 0028801044 scopus 로고
    • Advances in the use of Pichia pastoris for high-level gene expression
    • M.A. Romanos, Advances in the use of Pichia pastoris for high-level gene expression, Curr. Opion. Biotechnol. 6 (1995) 527-533.
    • (1995) Curr. Opion. Biotechnol. , vol.6 , pp. 527-533
    • Romanos, M.A.1
  • 20
    • 0028827506 scopus 로고
    • Review: Methylotrophic yeasts as factories for the production of foreign proteins
    • K.N. Faber, W. Harder, M. Veenhuis, Review: methylotrophic yeasts as factories for the production of foreign proteins, Yeast 14 (1995) 1331-1344.
    • (1995) Yeast , vol.14 , pp. 1331-1344
    • Faber, K.N.1    Harder, W.2    Veenhuis, M.3
  • 23
    • 0024701067 scopus 로고
    • Methylotrophic yeast Pichia pastoris produced in high-cell-density fermentations with high cell yields as vehicle for recombinant protein production
    • R.S. Siegel, R.A. Brierley, Methylotrophic yeast Pichia pastoris produced in high-cell-density fermentations with high cell yields as vehicle for recombinant protein production, Biotechnol. Bioeng. 34 (1989) 403-404.
    • (1989) Biotechnol. Bioeng. , vol.34 , pp. 403-404
    • Siegel, R.S.1    Brierley, R.A.2
  • 24
    • 0025168284 scopus 로고
    • Fermentation development of recombinant Pichia pastoris expressing the heterologe gene: Bovine lysozyme
    • R.A. Brierley, C. Bussineau, R. Kosson, A. Melton, R.S. Siegel, Fermentation development of recombinant Pichia pastoris expressing the heterologe gene: bovine lysozyme, Ann. NY Acad. Sci. 589 (1990) 350-362.
    • (1990) Ann. NY Acad. Sci. , vol.589 , pp. 350-362
    • Brierley, R.A.1    Bussineau, C.2    Kosson, R.3    Melton, A.4    Siegel, R.S.5
  • 26
    • 0342656487 scopus 로고    scopus 로고
    • Expression of the Arabidopsis thaliana AtJ2 cochaperone
    • R. Zhou, B. Kroczynska, J.A. Miernyk, Expression of the Arabidopsis thaliana AtJ2 cochaperone, Protein Expr. Purif. 19 (2000) 253-258.
    • (2000) Protein Expr. Purif. , vol.19 , pp. 253-258
    • Zhou, R.1    Kroczynska, B.2    Miernyk, J.A.3
  • 27
    • 2642582485 scopus 로고
    • Expression og human serum amyloid P component in COS-1 cells
    • S.C. Ying, K. Gupta, A.T. Gewurz, H. Gewurz, Expression og human serum amyloid P component in COS-1 cells, Clin. Res. 41 (1993) 671.
    • (1993) Clin. Res. , vol.41 , pp. 671
    • Ying, S.C.1    Gupta, K.2    Gewurz, A.T.3    Gewurz, H.4
  • 28
    • 0011246323 scopus 로고    scopus 로고
    • Electron microscopy of prefibrillar structures and amyloid fibrils
    • E. Holm Nielsen, M. Nybo, S.-E. Svehag, Electron microscopy of prefibrillar structures and amyloid fibrils, Methods Enzymol. 309 (1999) 491-496.
    • (1999) Methods Enzymol. , vol.309 , pp. 491-496
    • Holm Nielsen, E.1    Nybo, M.2    Svehag, S.-E.3
  • 29
    • 0021810987 scopus 로고
    • Human serum amyloid P component. cDNA isolation, complete sequence of pre-serum Amyloid P component, and localization of the gene to chromosome 1
    • E.C. Mantzouranis, S.B. Downton, A.S. Whitehead, M.D. Edge, G.A.P. Bruns, H.R. Colten, Human serum amyloid P component. cDNA isolation, complete sequence of pre-serum Amyloid P component, and localization of the gene to chromosome 1, J. Biol. Chem. 260 (1985) 7752-7756.
    • (1985) J. Biol. Chem. , vol.260 , pp. 7752-7756
    • Mantzouranis, E.C.1    Downton, S.B.2    Whitehead, A.S.3    Edge, M.D.4    Bruns, G.A.P.5    Colten, H.R.6
  • 31
    • 17744376367 scopus 로고    scopus 로고
    • Complexes of serum Amyloid P component and DNA in serum from healthy individuals and systemic lupus erythematosus patients
    • I. Juul Sørensen, E. Holm Nielsen, L. Schrader, A. Voss, L. Horváth, S.-E. Svehag, Complexes of serum Amyloid P component and DNA in serum from healthy individuals and systemic lupus erythematosus patients, J. Clin. Immunol. 20 (2000) 408-415.
    • (2000) J. Clin. Immunol. , vol.20 , pp. 408-415
    • Juul Sørensen, I.1    Holm Nielsen, E.2    Schrader, L.3    Voss, A.4    Horváth, L.5    Svehag, S.-E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.