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Volumn 15, Issue 3, 1999, Pages 362-369

Optimization of the production of a honeybee odorant-binding protein by Pichia pastoris

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; HONEYBEE; ION EXCHANGE CHROMATOGRAPHY; MASS SPECTROMETRY; MUTATIONAL ANALYSIS; ODORANT BINDING PROTEIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN STRUCTURE;

EID: 0033117364     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1998.1027     Document Type: Article
Times cited : (30)

References (37)
  • 2
    • 0040352690 scopus 로고
    • Odorant-binding protein: Localization to nasal glands and secretions
    • Pevsner J. Odorant-binding protein: Localization to nasal glands and secretions. Proc. Natl. Acad. Sci. USA. 83:1986;4942-4946.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4942-4946
    • Pevsner, J.1
  • 3
    • 0025259871 scopus 로고
    • Odorant-binding protein. Characterization of ligand binding
    • Pevsner J., Hou V., Snowman A. M., Snyder S. H. Odorant-binding protein. Characterization of ligand binding. J. Biol. Chem. 265:1990;6118-6125.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6118-6125
    • Pevsner, J.1    Hou, V.2    Snowman, A.M.3    Snyder, S.H.4
  • 4
    • 0029921089 scopus 로고    scopus 로고
    • Perireceptor events in olfaction
    • Pelosi P. Perireceptor events in olfaction. J. Neurobiol. 30:1996;3-19.
    • (1996) J. Neurobiol. , vol.30 , pp. 3-19
    • Pelosi, P.1
  • 5
    • 0029030309 scopus 로고
    • Odorant-binding proteins in insects
    • Pelosi P., Maida R. Odorant-binding proteins in insects. Comp. Biochem. Physiol. B. 111:1995;503-514.
    • (1995) Comp. Biochem. Physiol. B , vol.111 , pp. 503-514
    • Pelosi, P.1    Maida, R.2
  • 6
    • 0029958781 scopus 로고    scopus 로고
    • Peripheral mechanisms of pheromone reception in moths
    • Kaissling K. Peripheral mechanisms of pheromone reception in moths. Chem. Senses. 21:1996;257-268.
    • (1996) Chem. Senses , vol.21 , pp. 257-268
    • Kaissling, K.1
  • 7
    • 0031149741 scopus 로고    scopus 로고
    • Expression and characterization of a lepidopteran general odorant-binding protein
    • Feng L., Prestwich G. D. Expression and characterization of a lepidopteran general odorant-binding protein. Insect Biochem. Mol. Biol. 27:1997;405-412.
    • (1997) Insect Biochem. Mol. Biol. , vol.27 , pp. 405-412
    • Feng, L.1    Prestwich, G.D.2
  • 8
    • 0030822163 scopus 로고    scopus 로고
    • Biochemical characterization molecular cloning and localization of a putative odorant-binding protein in the honey beeApis mellifera
    • Danty E., Michard-Vanhée C., Huet J.-C., Genecque E., Pernollet J.-C., Masson C. Biochemical characterization molecular cloning and localization of a putative odorant-binding protein in the honey beeApis mellifera. FEBS Lett. 414:1997;595-598.
    • (1997) FEBS Lett. , vol.414 , pp. 595-598
    • Danty, E.1    Michard-Vanhée, C.2    Huet, J.-C.3    Genecque, E.4    Pernollet, J.-C.5    Masson, C.6
  • 9
    • 0031896322 scopus 로고    scopus 로고
    • Separation, characterization and sexual heterogeneity of multiple putative odorant-binding proteins in the honeybeeApis mellifera
    • Danty E., Arnold G., Huet J.-C., Huet D., Masson C., Pernollet J.-C. Separation, characterization and sexual heterogeneity of multiple putative odorant-binding proteins in the honeybeeApis mellifera. Chem. Senses. 23:1998;83-91.
    • (1998) Chem. Senses , vol.23 , pp. 83-91
    • Danty, E.1    Arnold, G.2    Huet, J.-C.3    Huet, D.4    Masson, C.5    Pernollet, J.-C.6
  • 10
    • 0027477528 scopus 로고
    • Bacterial expression and photoaffinity labeling of a pheromone binding protein
    • Prestwich G. D. Bacterial expression and photoaffinity labeling of a pheromone binding protein. Protein Sci. 2:1993;420-428.
    • (1993) Protein Sci. , vol.2 , pp. 420-428
    • Prestwich, G.D.1
  • 11
    • 0028278407 scopus 로고
    • Odorant binding by a pheromone binding protein:active site mapping by photoaffinity labeling
    • Du G., Ng C.-S., Prestwich G. D. Odorant binding by a pheromone binding protein:active site mapping by photoaffinity labeling. Biochemistry. 33:1994;4812-4819.
    • (1994) Biochemistry , vol.33 , pp. 4812-4819
    • Du, G.1    Ng, C.-S.2    Prestwich, G.D.3
  • 12
    • 0029067645 scopus 로고
    • Protein structure encodes the ligand binding specificity in pheromone binding proteins
    • Du G., Prestwich G. D. Protein structure encodes the ligand binding specificity in pheromone binding proteins. Biochemistry. 34:1995;8726-8732.
    • (1995) Biochemistry , vol.34 , pp. 8726-8732
    • Du, G.1    Prestwich, G.D.2
  • 13
    • 0026575323 scopus 로고
    • Expression of a pheromone-binding protein in insect cells using a baculovirus vector
    • Krieger J., Raming K., Prestwich G. D., Frith D., Stabel S., Breer H. Expression of a pheromone-binding protein in insect cells using a baculovirus vector. Eur. J. Biochem. 203:1992;161-166.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 161-166
    • Krieger, J.1    Raming, K.2    Prestwich, G.D.3    Frith, D.4    Stabel, S.5    Breer, H.6
  • 14
    • 0028774540 scopus 로고
    • Expression of highly disulfide-bonded proteins inPichia pastoris.
    • White C. E., Kempi N. M., Komives E. A. Expression of highly disulfide-bonded proteins inPichia pastoris. Structure. 2:1994;1003-1005.
    • (1994) Structure , vol.2 , pp. 1003-1005
    • White, C.E.1    Kempi, N.M.2    Komives, E.A.3
  • 17
    • 0028952523 scopus 로고
    • Antagonists of monocyte chemoattractant protein 1 identified by modification of functionally critical NH2-terminal residues
    • Gong J. H., Clark-Lewis I. Antagonists of monocyte chemoattractant protein 1 identified by modification of functionally critical NH2-terminal residues. J. Exp. Med. 181:1995;631-640.
    • (1995) J. Exp. Med. , vol.181 , pp. 631-640
    • Gong, J.H.1    Clark-Lewis, I.2
  • 18
    • 14744299579 scopus 로고
    • Recent advances in the expression of foreign genes inPichia pastoris.
    • Cregg J. M., Vedvick T. S., Raschke W. Recent advances in the expression of foreign genes inPichia pastoris. BioTechnology. 11:1993;905-910.
    • (1993) BioTechnology , vol.11 , pp. 905-910
    • Cregg, J.M.1    Vedvick, T.S.2    Raschke, W.3
  • 19
    • 0027129786 scopus 로고
    • High-level expression, purification and characterization of the Kunitz type protease inhibitor domain of protease nexin-2/amyloid β-protein precursor
    • Wagner S. L., Siegel R. S., Vedvick T. S., Raschke W. C., Van Nostrand W. E. High-level expression, purification and characterization of the Kunitz type protease inhibitor domain of protease nexin-2/amyloid β-protein precursor. Biochem. Biophys. Res. Commun. 186:1992;1138-1145.
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 1138-1145
    • Wagner, S.L.1    Siegel, R.S.2    Vedvick, T.S.3    Raschke, W.C.4    Van Nostrand, W.E.5
  • 21
    • 0028568061 scopus 로고
    • Expression, purification and characterization of the Kunitz type proteinase inhibitor domain of the amyloid β-protein precursor like protein-2
    • Van Nostrand W. E., Schmaier A. H., Neiditch B. R., Siegel R. S., Raschke W. C., Sisodia S. S., Eagner S. L. Expression, purification and characterization of the Kunitz type proteinase inhibitor domain of the amyloid β-protein precursor like protein-2. Biochim. Biophys. Acta. 1209:1994;165-170.
    • (1994) Biochim. Biophys. Acta , vol.1209 , pp. 165-170
    • Van Nostrand, W.E.1    Schmaier, A.H.2    Neiditch, B.R.3    Siegel, R.S.4    Raschke, W.C.5    Sisodia, S.S.6    Eagner, S.L.7
  • 22
    • 0028944846 scopus 로고
    • Eneration of rabbit monoclonal antibody fragment from combinatorial phage display library and their production in the yeastPichia pastoris.
    • Ridder R., Schmitz R., Legay Y. F., Gram H. eneration of rabbit monoclonal antibody fragment from combinatorial phage display library and their production in the yeastPichia pastoris. BioTechnology. 13:1995;255-260.
    • (1995) BioTechnology , vol.13 , pp. 255-260
    • Ridder, R.1    Schmitz, R.2    Legay, Y.F.3    Gram, H.4
  • 25
    • 0030475733 scopus 로고    scopus 로고
    • Production and purification of recombinant hirudin expressed in the methylotrophic yeastPichia pastoris.
    • Rosenfeld S. A., Nadeau D., Tiradeau J., Hollis G. F., Knabb R. M., Ja S. Production and purification of recombinant hirudin expressed in the methylotrophic yeastPichia pastoris. Protein Express. Purif. 8:1996;476-482.
    • (1996) Protein Express. Purif. , vol.8 , pp. 476-482
    • Rosenfeld, S.A.1    Nadeau, D.2    Tiradeau, J.3    Hollis, G.F.4    Knabb, R.M.5    Ja, S.6
  • 26
    • 0029443619 scopus 로고
    • Expression of a synthetic gene encoding the anticoagulant-antimetastatic protein ghilanten by the methylotrophic yeastPichia pastoris.
    • Brankamp R. G., Sreekrishna K., Smith P. L., Blankenship D. T., Cardin A. D. Expression of a synthetic gene encoding the anticoagulant-antimetastatic protein ghilanten by the methylotrophic yeastPichia pastoris. Protein Express. Purif. 6:1995;813-820.
    • (1995) Protein Express. Purif. , vol.6 , pp. 813-820
    • Brankamp, R.G.1    Sreekrishna, K.2    Smith, P.L.3    Blankenship, D.T.4    Cardin, A.D.5
  • 28
    • 0030444332 scopus 로고    scopus 로고
    • Expression, purification and characterization of recombinant α-NPichia pastoris.
    • Zhu A., Monahan C., Wang Z.-K., Goldstein J. Expression, purification and characterization of recombinant α-NPichia pastoris. Protein Express. Purif. 8:1996;456-462.
    • (1996) Protein Express. Purif. , vol.8 , pp. 456-462
    • Zhu, A.1    Monahan, C.2    Wang, Z.-K.3    Goldstein, J.4
  • 29
    • 0003149190 scopus 로고
    • Protocol for efficient secretion of HSA developed fromPichia pastoris.
    • Barr K. A., Hopkins S. A., Sreekrishna K. Protocol for efficient secretion of HSA developed fromPichia pastoris. Pharm. Eng. 12:1992;48-51.
    • (1992) Pharm. Eng. , vol.12 , pp. 48-51
    • Barr, K.A.1    Hopkins, S.A.2    Sreekrishna, K.3
  • 30
    • 0023484416 scopus 로고
    • Invertase gene (SUC2) ofSaccharomyces cerevisiaePichia pastoris.
    • Sreekrishna K., Tschopp J. F., Fluke M. Invertase gene (SUC2) ofSaccharomyces cerevisiaePichia pastoris. Gene. 59:1987;115-125.
    • (1987) Gene , vol.59 , pp. 115-125
    • Sreekrishna, K.1    Tschopp, J.F.2    Fluke, M.3
  • 31
    • 0000823705 scopus 로고
    • High-level secretion of glycosylated invertase in the methylotrophic yeast,Pichia pastoris.
    • Tschopp J. F., Svelow G., Kosson R., Craik W., Grinna L. High-level secretion of glycosylated invertase in the methylotrophic yeast,Pichia pastoris. BioTechnology. 5:1987;1305-1308.
    • (1987) BioTechnology , vol.5 , pp. 1305-1308
    • Tschopp, J.F.1    Svelow, G.2    Kosson, R.3    Craik, W.4    Grinna, L.5
  • 33
    • 0030696109 scopus 로고    scopus 로고
    • Expression and processing of vertebrate acetylcholinesterase in the yeastPichia pastoris.
    • Morel N., Massoulié J. Expression and processing of vertebrate acetylcholinesterase in the yeastPichia pastoris. Biochem. J. 328:1997;121-129.
    • (1997) Biochem. J. , vol.328 , pp. 121-129
    • Morel, N.1    Massoulié, J.2
  • 35
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 kDa to 100 kDa
    • Schägger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 kDa to 100 kDa. Anal. Biochem. 166:1987;368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 36
    • 0025266954 scopus 로고
    • Reassessment of commercially available molecular weight standards for peptide sodium dodecyl sulfate-polyacrylamide gel electrophoresis using electroblotting and microsequencing
    • Sallantin M., Huet J.-C., Demarteau C., Pernollet J.-C. Reassessment of commercially available molecular weight standards for peptide sodium dodecyl sulfate-polyacrylamide gel electrophoresis using electroblotting and microsequencing. Electrophoresis. 11:1990;34-36.
    • (1990) Electrophoresis , vol.11 , pp. 34-36
    • Sallantin, M.1    Huet, J.-C.2    Demarteau, C.3    Pernollet, J.-C.4
  • 37
    • 49749177569 scopus 로고
    • A colorimetric method for determining low concentrations of mercaptans
    • Ellman G. L. A colorimetric method for determining low concentrations of mercaptans. Arch. Biochem. Biophys. 74:1958;443-450.
    • (1958) Arch. Biochem. Biophys. , vol.74 , pp. 443-450
    • Ellman, G.L.1


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