메뉴 건너뛰기




Volumn 55, Issue 1, 2007, Pages 147-158

Expression of the Trichoderma reesei tyrosinase 2 in Pichia pastoris: Isotopic labeling and physicochemical characterization

Author keywords

Cu enzymes; Heterologous expression; NMR; Pichia pastoris; Tyrosinase

Indexed keywords

COPPER; MONOPHENOL MONOOXYGENASE; NITROGEN; RECOMBINANT PROTEIN;

EID: 34547856995     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2007.04.014     Document Type: Article
Times cited : (19)

References (66)
  • 1
    • 85053591293 scopus 로고
    • Tyrosinase
    • Lontie R. (Ed), CRC Press Inc., Boca Raton, FL
    • Robb D.A. Tyrosinase. In: Lontie R. (Ed). Copperproteins and Copper Enzymes vol. 2 (1984), CRC Press Inc., Boca Raton, FL 207-240
    • (1984) Copperproteins and Copper Enzymes , vol.2 , pp. 207-240
    • Robb, D.A.1
  • 2
    • 0022620642 scopus 로고
    • Different origins of metal binding sites in binuclear copper proteins, tyrosinase and hemocyanin
    • Lerch K., Huber M., Schneider H., Drexel R., and Linzen B. Different origins of metal binding sites in binuclear copper proteins, tyrosinase and hemocyanin. J. Inorg. Biochem. 26 (1986) 213-217
    • (1986) J. Inorg. Biochem. , vol.26 , pp. 213-217
    • Lerch, K.1    Huber, M.2    Schneider, H.3    Drexel, R.4    Linzen, B.5
  • 3
    • 0025885768 scopus 로고
    • Enzymatic control of pigmentation in mammals
    • Hearing V.J., and Tsukamoto K. Enzymatic control of pigmentation in mammals. FASEB J. 5 (1991) 2902-2909
    • (1991) FASEB J. , vol.5 , pp. 2902-2909
    • Hearing, V.J.1    Tsukamoto, K.2
  • 4
    • 0030007345 scopus 로고    scopus 로고
    • Tyrosinase and related proteins in mammalian pigmentation
    • del Marmol V., and Beermann F. Tyrosinase and related proteins in mammalian pigmentation. FEBS Lett. 381 (1996) 165-168
    • (1996) FEBS Lett. , vol.381 , pp. 165-168
    • del Marmol, V.1    Beermann, F.2
  • 5
    • 0043193607 scopus 로고
    • In vitro studies of 2,4-dihydroxyphenylalanine, a prodrug targeted against malignant melanoma cells
    • Morrison M.E., Yagi M.J., and Cohen G. In vitro studies of 2,4-dihydroxyphenylalanine, a prodrug targeted against malignant melanoma cells. Proc. Natl. Acad. Sci. USA 82 (1985) 2960-2964
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 2960-2964
    • Morrison, M.E.1    Yagi, M.J.2    Cohen, G.3
  • 6
    • 0032860282 scopus 로고    scopus 로고
    • Melanocyte directed enzyme prodrug therapy (MDEPT): development of a targeted treatment for malignant melanoma
    • Jordan A.M., Khan T.H., Osborn H.M., Photiou A., and Riley P.A. Melanocyte directed enzyme prodrug therapy (MDEPT): development of a targeted treatment for malignant melanoma. Bioorg. Med. Chem. 7 (1999) 1775-1780
    • (1999) Bioorg. Med. Chem. , vol.7 , pp. 1775-1780
    • Jordan, A.M.1    Khan, T.H.2    Osborn, H.M.3    Photiou, A.4    Riley, P.A.5
  • 7
    • 0034936580 scopus 로고    scopus 로고
    • Melanocyte-directed enzyme prodrug therapy (MDEPT). Development of second generation prodrugs for targeted treatment of malignant melanoma
    • Jordan A.M., Khan T.H., Malkin H., Osborn H.M., Photiou A., and Riley P.A. Melanocyte-directed enzyme prodrug therapy (MDEPT). Development of second generation prodrugs for targeted treatment of malignant melanoma. Bioorg. Med. Chem. 9 (2001) 1549-1558
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 1549-1558
    • Jordan, A.M.1    Khan, T.H.2    Malkin, H.3    Osborn, H.M.4    Photiou, A.5    Riley, P.A.6
  • 8
    • 0020688520 scopus 로고
    • Neurospora tyrosinase: structural, spectroscopic and catalytic properties
    • Lerch K. Neurospora tyrosinase: structural, spectroscopic and catalytic properties. Mol. Cell. Biochem. 52 (1983) 125-138
    • (1983) Mol. Cell. Biochem. , vol.52 , pp. 125-138
    • Lerch, K.1
  • 9
    • 46149132278 scopus 로고
    • Polyphenol oxidases in plant-recent progress
    • Mayer A.M. Polyphenol oxidases in plant-recent progress. Phytochemistry 26 (1987) 11-20
    • (1987) Phytochemistry , vol.26 , pp. 11-20
    • Mayer, A.M.1
  • 10
    • 0031900371 scopus 로고    scopus 로고
    • Diphenol oxidases, enzyme-catalysed browning and plant disease resistance
    • Walker J.R., and Ferrar P.H. Diphenol oxidases, enzyme-catalysed browning and plant disease resistance. Biotechnol. Genet. Eng. Rev. 15 (1998) 457-498
    • (1998) Biotechnol. Genet. Eng. Rev. , vol.15 , pp. 457-498
    • Walker, J.R.1    Ferrar, P.H.2
  • 11
    • 0000034469 scopus 로고
    • The biochemistry and control of enzymatic browning
    • Martínez M.V., and Whitaker J.R. The biochemistry and control of enzymatic browning. Trends Food Sci. Techn. 6 (1995) 195-200
    • (1995) Trends Food Sci. Techn. , vol.6 , pp. 195-200
    • Martínez, M.V.1    Whitaker, J.R.2
  • 12
    • 18944389755 scopus 로고    scopus 로고
    • Polyphenol oxidase
    • Whitaker J.R., Voragen A.G.J., and Wong D.W.S. (Eds), Marcel Dekker Inc., New York
    • Ramirez E.C., Whitaker J.R., and Virador V.M. Polyphenol oxidase. In: Whitaker J.R., Voragen A.G.J., and Wong D.W.S. (Eds). Handbook of Food Enzymology (2003), Marcel Dekker Inc., New York 509-523
    • (2003) Handbook of Food Enzymology , pp. 509-523
    • Ramirez, E.C.1    Whitaker, J.R.2    Virador, V.M.3
  • 13
    • 34247094456 scopus 로고    scopus 로고
    • Tyrosinase-catalyzed grafting of sericin peptides onto chitosan and production of protein-polysaccharide bioconjugates
    • Anghileri A., Lantto R., Kruus K., Arosio C., and Freddi G. Tyrosinase-catalyzed grafting of sericin peptides onto chitosan and production of protein-polysaccharide bioconjugates. J. Biotechnol. 127 (2007) 508-519
    • (2007) J. Biotechnol. , vol.127 , pp. 508-519
    • Anghileri, A.1    Lantto, R.2    Kruus, K.3    Arosio, C.4    Freddi, G.5
  • 14
    • 34249853658 scopus 로고    scopus 로고
    • Tyrosinase-aided protein cross-linking: effects on gel formation of chicken breast myofibrils and texture and water-holding of chicken breast meat homogenate gels
    • Lantto R., Puolanne E., Kruus K., Buchert J., and Autio K. Tyrosinase-aided protein cross-linking: effects on gel formation of chicken breast myofibrils and texture and water-holding of chicken breast meat homogenate gels. J. Agric. Food Chem. 55 (2007) 1248-1255
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 1248-1255
    • Lantto, R.1    Puolanne, E.2    Kruus, K.3    Buchert, J.4    Autio, K.5
  • 15
    • 0031760504 scopus 로고    scopus 로고
    • Crystal structure of a plant catechol oxidase containing a dicopper center
    • Klabunde T., Eicken C., Sacchettini J.C., and Krebs B. Crystal structure of a plant catechol oxidase containing a dicopper center. Nat. Struct. Biol. 5 (1998) 1084-1090
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1084-1090
    • Klabunde, T.1    Eicken, C.2    Sacchettini, J.C.3    Krebs, B.4
  • 16
    • 0036009142 scopus 로고    scopus 로고
    • The crystal structure of catechol oxidase: new insight into the function of type-3 copper proteins
    • Gerdemann C., Eicken C., and Krebs B. The crystal structure of catechol oxidase: new insight into the function of type-3 copper proteins. Acc. Chem. Res. 35 (2002) 183-191
    • (2002) Acc. Chem. Res. , vol.35 , pp. 183-191
    • Gerdemann, C.1    Eicken, C.2    Krebs, B.3
  • 17
    • 29344448672 scopus 로고    scopus 로고
    • Comparative analysis of polyphenol oxidase from plant and fungal species
    • Marusek C.M., Trobaugh N.M., Flurkey W.H., and Inlow J.K. Comparative analysis of polyphenol oxidase from plant and fungal species. J. Inorg. Biochem. 100 (2006) 108-123
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 108-123
    • Marusek, C.M.1    Trobaugh, N.M.2    Flurkey, W.H.3    Inlow, J.K.4
  • 18
    • 33646827679 scopus 로고    scopus 로고
    • Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis
    • Matoba Y., Kumagai T., Yamamoto A., Yoshitsu H., and Sugiyama M. Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis. J. Biol. Chem. 281 (2006) 8981-8990
    • (2006) J. Biol. Chem. , vol.281 , pp. 8981-8990
    • Matoba, Y.1    Kumagai, T.2    Yamamoto, A.3    Yoshitsu, H.4    Sugiyama, M.5
  • 19
    • 33746291588 scopus 로고    scopus 로고
    • The first crystal structure of tyrosinase: all questions answered?
    • Decker H., Schweikardt T., and Tuczek F. The first crystal structure of tyrosinase: all questions answered?. Angew. Chem. Int. Ed. 45 (2006) 4546-4550
    • (2006) Angew. Chem. Int. Ed. , vol.45 , pp. 4546-4550
    • Decker, H.1    Schweikardt, T.2    Tuczek, F.3
  • 21
    • 33645716883 scopus 로고    scopus 로고
    • Cloning and characterization of a tyrosinase gene from the white-rot fungus Pycnoporus sanguineus, and overproduction of the recombinant protein in Aspergillus niger
    • Halaouli S., Record E., Casalot L., Hamdi M., Sigoillot J.C., Asther M., and Lomascolo A. Cloning and characterization of a tyrosinase gene from the white-rot fungus Pycnoporus sanguineus, and overproduction of the recombinant protein in Aspergillus niger. Appl. Microbiol. Biotechnol. 70 (2006) 580-589
    • (2006) Appl. Microbiol. Biotechnol. , vol.70 , pp. 580-589
    • Halaouli, S.1    Record, E.2    Casalot, L.3    Hamdi, M.4    Sigoillot, J.C.5    Asther, M.6    Lomascolo, A.7
  • 22
    • 1642321768 scopus 로고    scopus 로고
    • An efficient method for the overexpression and purification of active tyrosinase from Streptomyces castaneoglobisporus
    • Kohashi P.Y., Kumagai T., Matoba Y., Yamamoto A., Maruyama M., and Sugiyama M. An efficient method for the overexpression and purification of active tyrosinase from Streptomyces castaneoglobisporus. Protein Expr. Purif. 34 (2004) 202-207
    • (2004) Protein Expr. Purif. , vol.34 , pp. 202-207
    • Kohashi, P.Y.1    Kumagai, T.2    Matoba, Y.3    Yamamoto, A.4    Maruyama, M.5    Sugiyama, M.6
  • 23
    • 33748327047 scopus 로고    scopus 로고
    • Production and characterization of a secreted, C-terminally processed tyrosinase from the filamentous fungus Trichoderma reesei
    • Selinheimo E., Saloheimo M., Ahola E., Westerholm-Parvinen A., Kalkkinen N., Buchert J., and Kruus K. Production and characterization of a secreted, C-terminally processed tyrosinase from the filamentous fungus Trichoderma reesei. FEBS J. 273 (2006) 4322-4335
    • (2006) FEBS J. , vol.273 , pp. 4322-4335
    • Selinheimo, E.1    Saloheimo, M.2    Ahola, E.3    Westerholm-Parvinen, A.4    Kalkkinen, N.5    Buchert, J.6    Kruus, K.7
  • 24
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • Cereghino J.L., and Cregg J.M. Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol. Rev. 24 (2000) 45-66
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 25
    • 0030870312 scopus 로고    scopus 로고
    • NMR studies of a viral protein that mimics the regulators of complement activation
    • Wiles A.P., Shaw G., Bright J., Perczel A., Campbell I.D., and Barlow P.N. NMR studies of a viral protein that mimics the regulators of complement activation. J. Mol. Biol. 272 (1997) 253-265
    • (1997) J. Mol. Biol. , vol.272 , pp. 253-265
    • Wiles, A.P.1    Shaw, G.2    Bright, J.3    Perczel, A.4    Campbell, I.D.5    Barlow, P.N.6
  • 27
    • 0031761951 scopus 로고    scopus 로고
    • NMR analysis of the N-terminal SRCR domain of human CD5: engineering of a glycoprotein for superior characteristics in NMR experiments
    • McAlister M.S., Davis B., Pfuhl M., and Driscoll P.C. NMR analysis of the N-terminal SRCR domain of human CD5: engineering of a glycoprotein for superior characteristics in NMR experiments. Protein Eng. 11 (1998) 847-853
    • (1998) Protein Eng. , vol.11 , pp. 847-853
    • McAlister, M.S.1    Davis, B.2    Pfuhl, M.3    Driscoll, P.C.4
  • 29
    • 0032991055 scopus 로고    scopus 로고
    • High-level expression of uniformly 15N-labeled hen lysozyme in Pichia pastoris and identification of the site in hen lysozyme where phosphate ion binds using NMR measurements
    • Mine S., Ueda T., Hashimoto Y., Tanaka Y., and Imoto T. High-level expression of uniformly 15N-labeled hen lysozyme in Pichia pastoris and identification of the site in hen lysozyme where phosphate ion binds using NMR measurements. FEBS Lett. 448 (1999) 33-37
    • (1999) FEBS Lett. , vol.448 , pp. 33-37
    • Mine, S.1    Ueda, T.2    Hashimoto, Y.3    Tanaka, Y.4    Imoto, T.5
  • 31
    • 1442264832 scopus 로고    scopus 로고
    • Expression of the GM2-activator protein in the methylotrophic yeast Pichia pastoris, purification, isotopic labeling, and biophysical characterization
    • Wendeler M., Hoernschemeyer J., John M., Werth N., Schoeniger M., Lemm T., Hartmann R., Kessler H., and Sandhoff K. Expression of the GM2-activator protein in the methylotrophic yeast Pichia pastoris, purification, isotopic labeling, and biophysical characterization. Protein Expr. Purif. 34 (2004) 147-157
    • (2004) Protein Expr. Purif. , vol.34 , pp. 147-157
    • Wendeler, M.1    Hoernschemeyer, J.2    John, M.3    Werth, N.4    Schoeniger, M.5    Lemm, T.6    Hartmann, R.7    Kessler, H.8    Sandhoff, K.9
  • 32
    • 0028081167 scopus 로고
    • High-level secretion and very efficient isotopic labeling of tick anticoagulant peptide (TAP) expressed in the methylotrophic yeast, Pichia pastoris
    • Laroche Y., Storme V., De Meutter J., Messens J., and Lauwereys M. High-level secretion and very efficient isotopic labeling of tick anticoagulant peptide (TAP) expressed in the methylotrophic yeast, Pichia pastoris. Biotechnology 12 (1994) 1119-1124
    • (1994) Biotechnology , vol.12 , pp. 1119-1124
    • Laroche, Y.1    Storme, V.2    De Meutter, J.3    Messens, J.4    Lauwereys, M.5
  • 36
    • 0032587512 scopus 로고    scopus 로고
    • Production of large quantities of isotopically labeled protein in Pichia pastoris by fermentation
    • Wood M.J., and Komives E.A. Production of large quantities of isotopically labeled protein in Pichia pastoris by fermentation. J. Biomol. NMR 13 (1999) 149-159
    • (1999) J. Biomol. NMR , vol.13 , pp. 149-159
    • Wood, M.J.1    Komives, E.A.2
  • 38
    • 0034923785 scopus 로고    scopus 로고
    • An economical method for (15)N/(13)C isotopic labeling of proteins expressed in Pichia pastoris
    • Rodriguez E., and Krishna N.R. An economical method for (15)N/(13)C isotopic labeling of proteins expressed in Pichia pastoris. J. Biochem. 130 (2001) 19-22
    • (2001) J. Biochem. , vol.130 , pp. 19-22
    • Rodriguez, E.1    Krishna, N.R.2
  • 39
    • 0032869411 scopus 로고    scopus 로고
    • Heterologous expression of a deuterated membrane-integrated receptor and partial deuteration in methylotrophic yeasts
    • Massou S., Puech V., Talmont F., Demange P., Lindley N.D., Tropis M., and Milon A. Heterologous expression of a deuterated membrane-integrated receptor and partial deuteration in methylotrophic yeasts. J. Biomol. NMR 14 (1999) 231-239
    • (1999) J. Biomol. NMR , vol.14 , pp. 231-239
    • Massou, S.1    Puech, V.2    Talmont, F.3    Demange, P.4    Lindley, N.D.5    Tropis, M.6    Milon, A.7
  • 40
    • 0033816837 scopus 로고    scopus 로고
    • Expression of deuterium-isotope-labelled protein in the yeast Pichia pastoris for NMR studies
    • Morgan W.D., Kragt A., and Feeney J. Expression of deuterium-isotope-labelled protein in the yeast Pichia pastoris for NMR studies. J. Biomol. NMR 17 (2000) 337-347
    • (2000) J. Biomol. NMR , vol.17 , pp. 337-347
    • Morgan, W.D.1    Kragt, A.2    Feeney, J.3
  • 41
    • 0242432456 scopus 로고    scopus 로고
    • Development of a high-level expression system for deuterium-labeled human serum albumin
    • Tomida M., Kimura M., Kuwata K., Hayashi T., Okano Y., and Era S. Development of a high-level expression system for deuterium-labeled human serum albumin. Jpn. J. Physiol. 53 (2003) 65-69
    • (2003) Jpn. J. Physiol. , vol.53 , pp. 65-69
    • Tomida, M.1    Kimura, M.2    Kuwata, K.3    Hayashi, T.4    Okano, Y.5    Era, S.6
  • 42
    • 0029739169 scopus 로고    scopus 로고
    • Cloning of genes encoding alpha-l-arabinofuranosidase and beta-xylosidase from Trichoderma reesei by expression in Saccharomyces cerevisiae
    • Margolles-Clark E., Tenkanen M., Nakari-Setälä T., and Penttilä M. Cloning of genes encoding alpha-l-arabinofuranosidase and beta-xylosidase from Trichoderma reesei by expression in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 62 (1996) 3840-3846
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3840-3846
    • Margolles-Clark, E.1    Tenkanen, M.2    Nakari-Setälä, T.3    Penttilä, M.4
  • 43
    • 34547895251 scopus 로고    scopus 로고
    • D.R. Higgins, J.M. Gregg, in: J.M. Walker (Ed.), Pichia Protocols, Methods in Molecular Biology 103, vol. 103, Humana Press Inc., Totowa, New Jersey, 1998.
  • 44
    • 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 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 45
    • 0034672623 scopus 로고    scopus 로고
    • Kinesin subfamily UNC104 contains a FHA domain: boundaries and physicochemical characterization
    • Westerholm-Parvinen A., Vernos I., and Serrano L. Kinesin subfamily UNC104 contains a FHA domain: boundaries and physicochemical characterization. FEBS Lett. 486 (2000) 285-290
    • (2000) FEBS Lett. , vol.486 , pp. 285-290
    • Westerholm-Parvinen, A.1    Vernos, I.2    Serrano, L.3
  • 46
    • 0035715001 scopus 로고    scopus 로고
    • Low-temperature increases the yield of biologically active herring antifreeze protein in Pichia pastoris
    • Li Z., Xiong F., Lin Q., d'Anjou M., Daugulis A.J., Yang D.S., and Hew C.L. Low-temperature increases the yield of biologically active herring antifreeze protein in Pichia pastoris. Protein Expr. Purif. 21 (2001) 438-445
    • (2001) Protein Expr. Purif. , vol.21 , pp. 438-445
    • Li, Z.1    Xiong, F.2    Lin, Q.3    d'Anjou, M.4    Daugulis, A.J.5    Yang, D.S.6    Hew, C.L.7
  • 47
    • 2942627936 scopus 로고    scopus 로고
    • Temperature limited fed-batch technique for control of proteolysis in Pichia pastoris bioreactor cultures
    • Jahic M., Wallberg F., Bollok M., Garcia P., and Enfors S.O. Temperature limited fed-batch technique for control of proteolysis in Pichia pastoris bioreactor cultures. Microb. Cell. Fact. (2003) 2:6
    • (2003) Microb. Cell. Fact.
    • Jahic, M.1    Wallberg, F.2    Bollok, M.3    Garcia, P.4    Enfors, S.O.5
  • 48
    • 2942584928 scopus 로고    scopus 로고
    • Increasing secretion of a bivalent anti-T-cell immunotoxin by Pichia pastoris
    • Woo J.H., Liu Y.Y., Stavrou S., and Neville D.M. Increasing secretion of a bivalent anti-T-cell immunotoxin by Pichia pastoris. Appl. Environ. Microbiol. 70 (2004) 3370-3376
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 3370-3376
    • Woo, J.H.1    Liu, Y.Y.2    Stavrou, S.3    Neville, D.M.4
  • 49
    • 33744912792 scopus 로고    scopus 로고
    • Production of recombinant HIV-1 Nef (negative factor) protein using Pichia pastoris and a low-temperature fed-batch strategy
    • Siren N., Weegar J., Dahlbacka J., Kalkkinen N., Fagervik K., Leisola M., and von Weymarn N. Production of recombinant HIV-1 Nef (negative factor) protein using Pichia pastoris and a low-temperature fed-batch strategy. Biotechnol. Appl. Biochem. 44 (2006) 151-158
    • (2006) Biotechnol. Appl. Biochem. , vol.44 , pp. 151-158
    • Siren, N.1    Weegar, J.2    Dahlbacka, J.3    Kalkkinen, N.4    Fagervik, K.5    Leisola, M.6    von Weymarn, N.7
  • 51
    • 0042595684 scopus 로고    scopus 로고
    • Purification and some properties of tyrosinase from Aspergillus flavipes 56003
    • Gukasyan G.S. Purification and some properties of tyrosinase from Aspergillus flavipes 56003. Biochemistry (Mosc). 64 (1999) 417-420
    • (1999) Biochemistry (Mosc). , vol.64 , pp. 417-420
    • Gukasyan, G.S.1
  • 52
    • 13244258458 scopus 로고    scopus 로고
    • Characterization of a new tyrosinase from Pycnoporus species with high potential for food technological applications
    • Halaouli S., Asther M., Kruus K., Guo L., Hamdi M., Sigoillot J.C., Asther M., and Lomascolo A. Characterization of a new tyrosinase from Pycnoporus species with high potential for food technological applications. J. Appl. Microbiol. 98 (2005) 332-343
    • (2005) J. Appl. Microbiol. , vol.98 , pp. 332-343
    • Halaouli, S.1    Asther, M.2    Kruus, K.3    Guo, L.4    Hamdi, M.5    Sigoillot, J.C.6    Asther, M.7    Lomascolo, A.8
  • 53
    • 19344370279 scopus 로고    scopus 로고
    • An episomal expression vector for screening mutant gene libraries in Pichia pastoris
    • C Lee C., Williams T.G., Wong D.W., and Robertson G.H. An episomal expression vector for screening mutant gene libraries in Pichia pastoris. Plasmid 54 (2005) 80-85
    • (2005) Plasmid , vol.54 , pp. 80-85
    • C Lee, C.1    Williams, T.G.2    Wong, D.W.3    Robertson, G.H.4
  • 54
    • 0026094226 scopus 로고
    • Production of mouse epidermal growth factor in yeast: high-level secretion using Pichia pastoris strains containing multiple gene copies
    • Clare J.J., Romanos M.A., Rayment F.B., Rowedder J.E., Smith M.A., Payne M.M., Sreekrishna K., and Henwood C.A. Production of mouse epidermal growth factor in yeast: high-level secretion using Pichia pastoris strains containing multiple gene copies. Gene 105 (1991) 205-212
    • (1991) Gene , vol.105 , pp. 205-212
    • Clare, J.J.1    Romanos, M.A.2    Rayment, F.B.3    Rowedder, J.E.4    Smith, M.A.5    Payne, M.M.6    Sreekrishna, K.7    Henwood, C.A.8
  • 55
    • 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-tau
    • Sinha J., Plantz B.A., Inan M., and Meagher M.M. Causes of proteolytic degradation of secreted recombinant proteins produced in methylotrophic yeast Pichia pastoris: case study with recombinant ovine interferon-tau. Biotechnol. Bioeng. 89 (2005) 102-112
    • (2005) Biotechnol. Bioeng. , vol.89 , pp. 102-112
    • Sinha, J.1    Plantz, B.A.2    Inan, M.3    Meagher, M.M.4
  • 56
    • 2642696839 scopus 로고    scopus 로고
    • Laccase from the white-rot fungus Trametes versicolor: cDNA cloning of lcc1 and expression in Pichia pastoris
    • Jönsson L.J., Saloheimo M., and Penttilä M. Laccase from the white-rot fungus Trametes versicolor: cDNA cloning of lcc1 and expression in Pichia pastoris. Curr. Genet. 32 (1997) 425-430
    • (1997) Curr. Genet. , vol.32 , pp. 425-430
    • Jönsson, L.J.1    Saloheimo, M.2    Penttilä, M.3
  • 58
    • 0024971467 scopus 로고
    • Isolation and characterization of the tyrosinase gene from Neurospora crassa
    • Kupper U., Niedermann D.M., Travaglini G., and Lerch K. Isolation and characterization of the tyrosinase gene from Neurospora crassa. J. Biol. Chem. 264 (1989) 17250-17258
    • (1989) J. Biol. Chem. , vol.264 , pp. 17250-17258
    • Kupper, U.1    Niedermann, D.M.2    Travaglini, G.3    Lerch, K.4
  • 59
    • 0036435884 scopus 로고    scopus 로고
    • The disulphide mapping, folding and characterisation of recombinant Ber e 1, an allergenic protein, and SFA8, two sulphur-rich 2S plant albumins
    • Alcocer M.J., Murtagh G.J., Bailey K., Dumoulin M., Meseguer A.S., Parker M.J., and Archer D.B. The disulphide mapping, folding and characterisation of recombinant Ber e 1, an allergenic protein, and SFA8, two sulphur-rich 2S plant albumins. J. Mol. Biol. 324 (2002) 165-175
    • (2002) J. Mol. Biol. , vol.324 , pp. 165-175
    • Alcocer, M.J.1    Murtagh, G.J.2    Bailey, K.3    Dumoulin, M.4    Meseguer, A.S.5    Parker, M.J.6    Archer, D.B.7
  • 60
    • 2342476496 scopus 로고    scopus 로고
    • The expression and processing of two recombinant 2S albumins from soybean (Glycine max) in the yeast Pichia pastoris
    • Lin J., Fido R., Shewry P., Archer D.B., and Alcocer M.J. The expression and processing of two recombinant 2S albumins from soybean (Glycine max) in the yeast Pichia pastoris. Biochim. Biophys. Acta 1698 (2004) 203-212
    • (2004) Biochim. Biophys. Acta , vol.1698 , pp. 203-212
    • Lin, J.1    Fido, R.2    Shewry, P.3    Archer, D.B.4    Alcocer, M.J.5
  • 61
    • 0024637162 scopus 로고
    • Size distribution and general structural features of N-linked oligosaccharides from the methylotrophic yeast, Pichia pastoris
    • Grinna L.S., and Tschopp J.F. Size distribution and general structural features of N-linked oligosaccharides from the methylotrophic yeast, Pichia pastoris. Yeast 5 (1989) 107-115
    • (1989) Yeast , vol.5 , pp. 107-115
    • Grinna, L.S.1    Tschopp, J.F.2
  • 63
    • 0032959440 scopus 로고    scopus 로고
    • Overview of N- and O-linked oligosaccharide structures found in various yeast species
    • Gemmill T.R., and Trimble R.B. Overview of N- and O-linked oligosaccharide structures found in various yeast species. Biochim. Biophys. Acta 1426 (1999) 227-237
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 227-237
    • Gemmill, T.R.1    Trimble, R.B.2
  • 64
    • 33845587326 scopus 로고    scopus 로고
    • Characterization of the N-linked oligosaccharides from human chorionic gonadotropin expressed in the methylotrophic yeast Pichia pastoris
    • Blanchard V., Gadkari R.A., Gerwig G.J., Leeflang B.R., Dighe R.R., and Kamerling J.P. Characterization of the N-linked oligosaccharides from human chorionic gonadotropin expressed in the methylotrophic yeast Pichia pastoris. Glycoconj. J. 24 (2007) 33-47
    • (2007) Glycoconj. J. , vol.24 , pp. 33-47
    • Blanchard, V.1    Gadkari, R.A.2    Gerwig, G.J.3    Leeflang, B.R.4    Dighe, R.R.5    Kamerling, J.P.6
  • 66
    • 0036175914 scopus 로고    scopus 로고
    • NMR-based structural characterization of large protein-ligand interactions
    • Pellecchia M., Meininger D., Dong Q., Chang E., Jack R., and Sem D.S. NMR-based structural characterization of large protein-ligand interactions. J. Biomol. NMR 22 (2002) 165-173
    • (2002) J. Biomol. NMR , vol.22 , pp. 165-173
    • Pellecchia, M.1    Meininger, D.2    Dong, Q.3    Chang, E.4    Jack, R.5    Sem, D.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.