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Volumn 72, Issue 2, 2007, Pages

Expression and purification of goat lactoferrin from Pichia pastoris expression system

Author keywords

Expression; Gene cloning; Goat lactoferrin; Pichia pastoris; Recombinant lactoferrin

Indexed keywords

COMPLEMENTARY DNA; IRON; LACTOFERRIN; RECOMBINANT PROTEIN;

EID: 33847773184     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1750-3841.2007.00281.x     Document Type: Article
Times cited : (22)

References (38)
  • 1
    • 3342963515 scopus 로고    scopus 로고
    • Lactoferrin and iron: Structural and dynamic aspects of binding and release (Review)
    • Baker HM, Baker EN. 2004. Lactoferrin and iron: structural and dynamic aspects of binding and release (Review). Biometals 17:209-16.
    • (2004) Biometals , vol.17 , pp. 209-216
    • Baker, H.M.1    Baker, E.N.2
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principal of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principal of protein-dye binding. Anal Biochem 72:248-54.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0018132103 scopus 로고
    • Identification of lactoferrin as the granulocyte-derived inhibitor of colony stimulating activity (CSA)-production
    • Broxmeyer HE, Smithyman A, Eger RR, Meyers PA, de Sousa M. 1978. Identification of lactoferrin as the granulocyte-derived inhibitor of colony stimulating activity (CSA)-production. J Exp Med 148:1052-67.
    • (1978) J Exp Med , vol.148 , pp. 1052-1067
    • Broxmeyer, H.E.1    Smithyman, A.2    Eger, R.R.3    Meyers, P.A.4    de Sousa, M.5
  • 5
    • 0026628351 scopus 로고
    • Studies of the N-terminal half of human lactoferrin produced from the cloned cDNA demonstrate that interlobe interactions modulate iron release
    • Day CL, Stowell KM, Baker EN, Tweedie JW. 1992. Studies of the N-terminal half of human lactoferrin produced from the cloned cDNA demonstrate that interlobe interactions modulate iron release. J Biol Chem 267:13857-62.
    • (1992) J Biol Chem , vol.267 , pp. 13857-13862
    • Day, C.L.1    Stowell, K.M.2    Baker, E.N.3    Tweedie, J.W.4
  • 6
    • 0019467167 scopus 로고
    • Lactoferrin-mediated modulation of mononuclear cell activities
    • Duncan RH, McArthur WP. 1981. Lactoferrin-mediated modulation of mononuclear cell activities. Cell Immunol 63:308-20.
    • (1981) Cell Immunol , vol.63 , pp. 308-320
    • Duncan, R.H.1    McArthur, W.P.2
  • 7
    • 0014885534 scopus 로고
    • Sequence determination (Review)
    • Edman P. 1970. Sequence determination (Review). Mol Biol Biochem Biophys 8:211-55.
    • (1970) Mol Biol Biochem Biophys , vol.8 , pp. 211-255
    • Edman, P.1
  • 8
    • 0029867181 scopus 로고    scopus 로고
    • Altered domain closure and ironbinding in transferrins: The crystal structure of the Asp60Ser mutant of the amino-terminal half of human lactoferrin
    • Faber RH, Bland T, Day CL, Norris GE, Tweedie JW, Baker EN. 1996. Altered domain closure and ironbinding in transferrins: the crystal structure of the Asp60Ser mutant of the amino-terminal half of human lactoferrin. J Mol Biol 256:352-63.
    • (1996) J Mol Biol , vol.256 , pp. 352-363
    • Faber, R.H.1    Bland, T.2    Day, C.L.3    Norris, G.E.4    Tweedie, J.W.5    Baker, E.N.6
  • 9
    • 0021059044 scopus 로고
    • Identification of lactoferrin as an essential growth factor for human lymphocytic cell lines in serum-free medium
    • Hashizume S, Kuroda K, Murakami H. 1983. Identification of lactoferrin as an essential growth factor for human lymphocytic cell lines in serum-free medium. Biochim Biophys Acta 763:377-82.
    • (1983) Biochim Biophys Acta , vol.763 , pp. 377-382
    • Hashizume, S.1    Kuroda, K.2    Murakami, H.3
  • 10
    • 0022569859 scopus 로고
    • A rapid, efficient method for isolating DNA from yeast
    • Holm C, Meeks-wagner DW, Fangman WL, Botstein D. 1986. A rapid, efficient method for isolating DNA from yeast. Gene 42:169-73.
    • (1986) Gene , vol.42 , pp. 169-173
    • Holm, C.1    Meeks-wagner, D.W.2    Fangman, W.L.3    Botstein, D.4
  • 14
    • 0029130333 scopus 로고
    • Lactoferrin: Molecular structure and biological function
    • Lonnerdal B, Iyer S. 1995. Lactoferrin: molecular structure and biological function. Annu Rev Nutr 15:93-110.
    • (1995) Annu Rev Nutr , vol.15 , pp. 93-110
    • Lonnerdal, B.1    Iyer, S.2
  • 15
    • 0019153180 scopus 로고
    • Comparative study of the iron-binding properties of human tranferrins. I. Complete and sequential iron saturation and desaturation of the lactotransferrin
    • Mazurier J, Spik G. 1980. Comparative study of the iron-binding properties of human tranferrins. I. Complete and sequential iron saturation and desaturation of the lactotransferrin. Biochim Biophys Acta 629:399-408.
    • (1980) Biochim Biophys Acta , vol.629 , pp. 399-408
    • Mazurier, J.1    Spik, G.2
  • 16
    • 0024586305 scopus 로고
    • Expression of human lactotransferrin receptors in phytohemagglutinin-stimulated human peripheral blood lymphocytes. Isolation of the receptors by anti-ligand affinity chromatography
    • Mazurier J, Legrand D, Hu WL, Montreuil J, Spik G. 1989. Expression of human lactotransferrin receptors in phytohemagglutinin-stimulated human peripheral blood lymphocytes. Isolation of the receptors by anti-ligand affinity chromatography. Eur J Biochem 179:481-7.
    • (1989) Eur J Biochem , vol.179 , pp. 481-487
    • Mazurier, J.1    Legrand, D.2    Hu, W.L.3    Montreuil, J.4    Spik, G.5
  • 20
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • Neuhoff V, Arold N, Toube D, Ehrhardt W. 1988. Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 9:255-62.
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Toube, D.3    Ehrhardt, W.4
  • 21
    • 0031038477 scopus 로고    scopus 로고
    • Mutagenesis of the histidine ligand in human lactoferrin: Iron binding properties and crystal structure of the His253Met mutant
    • Nicholson H, Anderson BF, Bland T, Shewry SC, Tweedie JW, Baker EN. 1997. Mutagenesis of the histidine ligand in human lactoferrin: iron binding properties and crystal structure of the His253Met mutant. Biochemistry 36:3421-6.
    • (1997) Biochemistry , vol.36 , pp. 3421-3426
    • Nicholson, H.1    Anderson, B.F.2    Bland, T.3    Shewry, S.C.4    Tweedie, J.W.5    Baker, E.N.6
  • 25
    • 0000005187 scopus 로고
    • Plasmid vector
    • Sambrook J, Fritsch EF, Maniatis T, editors, 2nd ed. New York: Cold Spring Harbor Laboratory Press. p
    • Sambrook J, Fritsch EF, Maniatis T. 1989. Plasmid vector. In: Sambrook J, Fritsch EF, Maniatis T, editors. Molecular cloning: a laboratory manual. 2nd ed. New York: Cold Spring Harbor Laboratory Press. p 72-3.
    • (1989) Molecular cloning: A laboratory manual , pp. 72-73
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 26
  • 29
    • 0018179083 scopus 로고
    • Bacteriostasis of a milk-sensitive strain of Escherichia coli by immunoglobulins and iron-binding proteins in association
    • Spik G, Che'ron A, Montreuil J, Dolby J. 1978. Bacteriostasis of a milk-sensitive strain of Escherichia coli by immunoglobulins and iron-binding proteins in association. Immunology 35:663-71.
    • (1978) Immunology , vol.35 , pp. 663-671
    • Spik, G.1    Che'ron, A.2    Montreuil, J.3    Dolby, J.4
  • 30
    • 1342322699 scopus 로고    scopus 로고
    • The role of N-linked glycosylation in the protection of human and bovine lactoferrin against tryptic proteolysis
    • van Veen HA, Geerts ME, van Berkel PH, Nuijens JH. 2004. The role of N-linked glycosylation in the protection of human and bovine lactoferrin against tryptic proteolysis. Eur J Biochem 271:678-84.
    • (2004) Eur J Biochem , vol.271 , pp. 678-684
    • van Veen, H.A.1    Geerts, M.E.2    van Berkel, P.H.3    Nuijens, J.H.4
  • 31
    • 0036930691 scopus 로고    scopus 로고
    • Expression, characterization, and purification of recombinant porcine lactoferrin in Pichia pastoris
    • Wang SH, Yang TS, Lin SM, Tsai MS, Wu SC, Mao SJT. 2002. Expression, characterization, and purification of recombinant porcine lactoferrin in Pichia pastoris. Protein Expr Purif 25:41-9.
    • (2002) Protein Expr Purif , vol.25 , pp. 41-49
    • Wang, S.H.1    Yang, T.S.2    Lin, S.M.3    Tsai, M.S.4    Wu, S.C.5    Mao, S.J.T.6
  • 32
    • 0026448560 scopus 로고
    • An inducible expression system for the production of human lactoferrin in Aspergillus nidulans
    • Ward PP, May GS, Headon DR, Conneely OM. 1992. An inducible expression system for the production of human lactoferrin in Aspergillus nidulans. Gene 122:219-23.
    • (1992) Gene , vol.122 , pp. 219-223
    • Ward, P.P.1    May, G.S.2    Headon, D.R.3    Conneely, O.M.4
  • 33
    • 0031578704 scopus 로고    scopus 로고
    • Expression and characterization of recombinant murine lactoferrin
    • Ward PP, Chu H, Zhou X, Conneely OM. 1997. Expression and characterization of recombinant murine lactoferrin. Gene 204:171-6.
    • (1997) Gene , vol.204 , pp. 171-176
    • Ward, P.P.1    Chu, H.2    Zhou, X.3    Conneely, O.M.4
  • 34
    • 0034166581 scopus 로고    scopus 로고
    • Presence of a glycan at a potential N-glycosylation site, Asn-281, of bovine lactoferrin
    • Wei Z, Nishimura T, Yoshida S. 2000. Presence of a glycan at a potential N-glycosylation site, Asn-281, of bovine lactoferrin. J Dairy Sci 83:683-9.
    • (2000) J Dairy Sci , vol.83 , pp. 683-689
    • Wei, Z.1    Nishimura, T.2    Yoshida, S.3
  • 35
    • 0014548372 scopus 로고
    • Glycoprotein staining following electrophoresis on acrylamide gels
    • Zacharius RM, Zell TE, Morrison JH, Woodlock JJ. 1959. Glycoprotein staining following electrophoresis on acrylamide gels. Anal Chem 30:148-52.
    • (1959) Anal Chem , vol.30 , pp. 148-152
    • Zacharius, R.M.1    Zell, T.E.2    Morrison, J.H.3    Woodlock, J.J.4
  • 36
    • 0025914111 scopus 로고
    • Immunostimulatory activity of lactotransferrin and maturation of CD40CD80 murine thymocytes
    • Zimecki M, Mazurier J, Machnicki M, Wieczorek Z, Montreuil J, Spik G. 1991. Immunostimulatory activity of lactotransferrin and maturation of CD40CD80 murine thymocytes. Immunol Lett 30:119-24.
    • (1991) Immunol Lett , vol.30 , pp. 119-124
    • Zimecki, M.1    Mazurier, J.2    Machnicki, M.3    Wieczorek, Z.4    Montreuil, J.5    Spik, G.6
  • 37
    • 0029145713 scopus 로고
    • Human lactoferrin induces phenotypic and functional changes in murine splenic B cells
    • Zimecki M, Mazurier J, Spik G, Kapp JA. 1995. Human lactoferrin induces phenotypic and functional changes in murine splenic B cells. Immunology 86:122-7.
    • (1995) Immunology , vol.86 , pp. 122-127
    • Zimecki, M.1    Mazurier, J.2    Spik, G.3    Kapp, J.A.4
  • 38
    • 0024468617 scopus 로고
    • Lactoferrin decreases monocyte-induced fibroblast production of myeloid colony-stimulating activity by suppressing monocyte release of interleukin-1
    • Zucali JR, Broxmeyer HE, Levy D, Morse C. 1989. Lactoferrin decreases monocyte-induced fibroblast production of myeloid colony-stimulating activity by suppressing monocyte release of interleukin-1. Blood 74(5):1531-6.
    • (1989) Blood , vol.74 , Issue.5 , pp. 1531-1536
    • Zucali, J.R.1    Broxmeyer, H.E.2    Levy, D.3    Morse, C.4


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