메뉴 건너뛰기




Volumn 70, Issue 2, 2010, Pages 270-276

High-level soluble expression, purification and characterization of active human midkine from Escherichia coli

Author keywords

Affinity purification; Analysis; Disulfide bond; Escherichia coli expression; Human midkine

Indexed keywords

HYBRID PROTEIN; MDK PROTEIN, HUMAN; NERVE GROWTH FACTOR;

EID: 76749168492     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2009.10.015     Document Type: Article
Times cited : (10)

References (19)
  • 1
    • 0029548635 scopus 로고
    • Pleiotrophin and midkine in normal development and tumor biology
    • Kurtz A., Schulte A.M., and Wellstein A. Pleiotrophin and midkine in normal development and tumor biology. Crit. Rev. Oncog. 6 (1995) 151-177
    • (1995) Crit. Rev. Oncog. , vol.6 , pp. 151-177
    • Kurtz, A.1    Schulte, A.M.2    Wellstein, A.3
  • 2
    • 0023646017 scopus 로고
    • Isolation and some characteristics of an adhesive factor of brain that enhances neurite outgrowth in central neurons
    • Rauvala H., and Pihlaskari R. Isolation and some characteristics of an adhesive factor of brain that enhances neurite outgrowth in central neurons. J. Biol. Chem. 262 (1987) 16625-16635
    • (1987) J. Biol. Chem. , vol.262 , pp. 16625-16635
    • Rauvala, H.1    Pihlaskari, R.2
  • 3
    • 0036739307 scopus 로고    scopus 로고
    • Midkine and pleiotrophin: two related proteins involved in development, survival, inflammation and tumorigenesis
    • Muramatsu T. Midkine and pleiotrophin: two related proteins involved in development, survival, inflammation and tumorigenesis. J. Biochem. 132 (2002) 359-371
    • (2002) J. Biochem. , vol.132 , pp. 359-371
    • Muramatsu, T.1
  • 5
    • 0842265835 scopus 로고    scopus 로고
    • Midkine and pleiotrophin in neural development and cancer
    • Kadomatsu K., and Muramatsu T. Midkine and pleiotrophin in neural development and cancer. Cancer Lett. 204 (2004) 127-143
    • (2004) Cancer Lett. , vol.204 , pp. 127-143
    • Kadomatsu, K.1    Muramatsu, T.2
  • 6
    • 0025800487 scopus 로고
    • Purification of recombinant midkine and examination of its biological activities: functional comparison of new heparin binding factors
    • Muramatsu H., and Muramatsu T. Purification of recombinant midkine and examination of its biological activities: functional comparison of new heparin binding factors. Biochem. Biophys. Res. Commun. 177 (1991) 652-658
    • (1991) Biochem. Biophys. Res. Commun. , vol.177 , pp. 652-658
    • Muramatsu, H.1    Muramatsu, T.2
  • 7
    • 59249090274 scopus 로고    scopus 로고
    • Midkine translocated to nucleoli and involved in carcinogenesis
    • Dai L.C. Midkine translocated to nucleoli and involved in carcinogenesis. World J. Gastroenterol. 15 (2009) 412-416
    • (2009) World J. Gastroenterol. , vol.15 , pp. 412-416
    • Dai, L.C.1
  • 8
    • 0034028190 scopus 로고    scopus 로고
    • Solution synthesis and biological activity if human pleotrophin, a novel heparin-binding neurotrophic factor consisting of 136 amino acid residues with five disulfide bonds
    • Inui T., Nakao M., Nishio H., Nishiuchi Y., Kojima S., Muramatusu T., and Kimura T. Solution synthesis and biological activity if human pleotrophin, a novel heparin-binding neurotrophic factor consisting of 136 amino acid residues with five disulfide bonds. J. Pept. Res. 55 (2000) 384-397
    • (2000) J. Pept. Res. , vol.55 , pp. 384-397
    • Inui, T.1    Nakao, M.2    Nishio, H.3    Nishiuchi, Y.4    Kojima, S.5    Muramatusu, T.6    Kimura, T.7
  • 9
    • 0027250183 scopus 로고
    • Structural characterisation of native and recombinant forms of the neurotrophic cytokine MK
    • Fabri L., and Maruta H. Structural characterisation of native and recombinant forms of the neurotrophic cytokine MK. J. Chromatogr. 646 (1993) 213-226
    • (1993) J. Chromatogr. , vol.646 , pp. 213-226
    • Fabri, L.1    Maruta, H.2
  • 10
    • 0031157025 scopus 로고    scopus 로고
    • Molecular chaperons, folding catalysis, and the recovery of active recombinant proteins from E. coli to fold or refold
    • Thomas J.G., Aylingand A., and Baneyx F. Molecular chaperons, folding catalysis, and the recovery of active recombinant proteins from E. coli to fold or refold. Appl. Biochem. Biotechnol. 66 (1997) 197-238
    • (1997) Appl. Biochem. Biotechnol. , vol.66 , pp. 197-238
    • Thomas, J.G.1    Aylingand, A.2    Baneyx, F.3
  • 13
    • 62249203623 scopus 로고    scopus 로고
    • Expression and purification of bioactive high-purity human midkine in Escherichia coli
    • Zhang Z., Du L., Xiang D., Zhu S., Wu M., Lu H., Yu Y., and Han W. Expression and purification of bioactive high-purity human midkine in Escherichia coli. J. Zhejinag Univ. Sci. 10 (2009) 79-86
    • (2009) J. Zhejinag Univ. Sci. , vol.10 , pp. 79-86
    • Zhang, Z.1    Du, L.2    Xiang, D.3    Zhu, S.4    Wu, M.5    Lu, H.6    Yu, Y.7    Han, W.8
  • 14
    • 0037298461 scopus 로고    scopus 로고
    • Production of native recombinant human midkine in the yeast, Pichia pastoris
    • Murasugo A., and Tohma-Aiba Y. Production of native recombinant human midkine in the yeast, Pichia pastoris. Protein Expr. Purif. 27 (2003) 244-252
    • (2003) Protein Expr. Purif. , vol.27 , pp. 244-252
    • Murasugo, A.1    Tohma-Aiba, Y.2
  • 15
    • 0027739665 scopus 로고
    • Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli
    • Derman A.I., Prinz W.A., Belin D., and Beckwith J. Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science 262 (1993) 1744-1747
    • (1993) Science , vol.262 , pp. 1744-1747
    • Derman, A.I.1    Prinz, W.A.2    Belin, D.3    Beckwith, J.4
  • 16
    • 14844334893 scopus 로고    scopus 로고
    • Solubility of disulfide-bonded proteins in the cytoplasm of Escherichia coli and its "oxidizing" mutant
    • Xiong S., Wang Y.F., Ren X.R., Zhang M.Y., Luo Y., Zhang L., Xie Q.L., and Su K.Y. Solubility of disulfide-bonded proteins in the cytoplasm of Escherichia coli and its "oxidizing" mutant. World J. Gastroenterol. 11 (2005) 1077-1082
    • (2005) World J. Gastroenterol. , vol.11 , pp. 1077-1082
    • Xiong, S.1    Wang, Y.F.2    Ren, X.R.3    Zhang, M.Y.4    Luo, Y.5    Zhang, L.6    Xie, Q.L.7    Su, K.Y.8
  • 17
    • 0034966491 scopus 로고    scopus 로고
    • Accurate disulfide formation in Escherichia coli overexpression and characterization of the first domain (HF6478) of the multiple Kazal-type inhibitor LEKT1
    • Lauber T., Marx U.C., Schulz A., Kreutzmann P., Rosch P., and Hoffmann S. Accurate disulfide formation in Escherichia coli overexpression and characterization of the first domain (HF6478) of the multiple Kazal-type inhibitor LEKT1. Protein Expr. Purif. 22 (2001) 108-122
    • (2001) Protein Expr. Purif. , vol.22 , pp. 108-122
    • Lauber, T.1    Marx, U.C.2    Schulz, A.3    Kreutzmann, P.4    Rosch, P.5    Hoffmann, S.6
  • 18
    • 33847096760 scopus 로고    scopus 로고
    • Cox17, a copper chaperone for cytochrome c oxidase: expression, purification, and formation of mixed disulfide adducts with thiol reagents
    • Voronova A., Kazantseva J., Tuuling M., Sokolova N., Sillard R., and Palumaa P. Cox17, a copper chaperone for cytochrome c oxidase: expression, purification, and formation of mixed disulfide adducts with thiol reagents. Protein Expr. Purif. 53 (2006) 138-144
    • (2006) Protein Expr. Purif. , vol.53 , pp. 138-144
    • Voronova, A.1    Kazantseva, J.2    Tuuling, M.3    Sokolova, N.4    Sillard, R.5    Palumaa, P.6
  • 19
    • 0023722548 scopus 로고
    • Complex regulation and functional versatility of mammalian alpha- and beta-tubulin isotypes during differentiation of testis and muscle cells
    • Lewis S.A., and Cowan N.J. Complex regulation and functional versatility of mammalian alpha- and beta-tubulin isotypes during differentiation of testis and muscle cells. J. Cell Biol. 106 (1988) 2023-2033
    • (1988) J. Cell Biol. , vol.106 , pp. 2023-2033
    • Lewis, S.A.1    Cowan, N.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.