메뉴 건너뛰기




Volumn 85, Issue 6, 2004, Pages 601-609

Optimized Procedure for Renaturation of Recombinant Human Bone Morphogenetic Protein-2 at High Protein Concentration

Author keywords

Bone morphogenetic protein 2; Escherichia coli; Renaturation

Indexed keywords

AMINO ACIDS; GENETIC ENGINEERING; PH EFFECTS; PROTEINS; REDOX REACTIONS;

EID: 1442350517     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.10906     Document Type: Article
Times cited : (77)

References (34)
  • 3
    • 0026792807 scopus 로고
    • A method for increasing the yield of properly folded recombinant fusion proteins: Single-chain immunotoxins from renaturation of bacterial inclusion bodies
    • Buchner J, Pastan I, Brinkmann U. 1992. A method for increasing the yield of properly folded recombinant fusion proteins: single-chain immunotoxins from renaturation of bacterial inclusion bodies. Anal Biochem 205:263-270.
    • (1992) Anal Biochem , vol.205 , pp. 263-270
    • Buchner, J.1    Pastan, I.2    Brinkmann, U.3
  • 5
    • 0032855077 scopus 로고    scopus 로고
    • Inhibition of aggregation side reactions during in vitro protein folding
    • De Bernardez Clark E, Schwarz E, Rudolph R. 1999. Inhibition of aggregation side reactions during in vitro protein folding. Methods Enzymol 309:217-236.
    • (1999) Methods Enzymol , vol.309 , pp. 217-236
    • De Bernardez Clark, E.1    Schwarz, E.2    Rudolph, R.3
  • 6
    • 0026658365 scopus 로고
    • A novel sequential procedure to enhance the renaturation of recombinant protein from Escherichia coli inclusion bodies
    • Fischer B, Perry B, Sumner I, Goodenough P. 1992. A novel sequential procedure to enhance the renaturation of recombinant protein from Escherichia coli inclusion bodies. Protein Eng 5:593-596.
    • (1992) Protein Eng , vol.5 , pp. 593-596
    • Fischer, B.1    Perry, B.2    Sumner, I.3    Goodenough, P.4
  • 7
    • 1842410676 scopus 로고    scopus 로고
    • Oxidative renaturation of lysozyme at high concentrations
    • Hevehan DL, De Bernardez Clark E. 1997. Oxidative renaturation of lysozyme at high concentrations. Biotechnol Bioeng 54:221-230.
    • (1997) Biotechnol Bioeng , vol.54 , pp. 221-230
    • Hevehan, D.L.1    De Bernardez Clark, E.2
  • 8
    • 0029737070 scopus 로고    scopus 로고
    • Bone morphogenetic proteins: Multifunctional regulators of vertebrate development
    • Hogan BLM. 1996. Bone morphogenetic proteins: multifunctional regulators of vertebrate development. Genes Dev 10:1580-1594.
    • (1996) Genes Dev , vol.10 , pp. 1580-1594
    • Hogan, B.L.M.1
  • 9
    • 0034210193 scopus 로고    scopus 로고
    • Direct refolding of recombinant human growth differentiation factor 5 for large-scale production process
    • Honda J, Andou H, Mannen T, Sugimoto S. 2000. Direct refolding of recombinant human growth differentiation factor 5 for large-scale production process. J Biosci Bioeng 89:582-589.
    • (2000) J Biosci Bioeng , vol.89 , pp. 582-589
    • Honda, J.1    Andou, H.2    Mannen, T.3    Sugimoto, S.4
  • 10
    • 0026640324 scopus 로고
    • Expression and characterization of bone morphogenetic protein-2 in Chinese hamster ovary cells
    • Israel DI, Nove J, Kerns KM, Moutsatsos IK, Kaufman RJ. 1992. Expression and characterization of bone morphogenetic protein-2 in Chinese hamster ovary cells. Growth Factors 7:139-150.
    • (1992) Growth Factors , vol.7 , pp. 139-150
    • Israel, D.I.1    Nove, J.2    Kerns, K.M.3    Moutsatsos, I.K.4    Kaufman, R.J.5
  • 11
    • 0028804911 scopus 로고
    • Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli
    • Kane JF. 1995. Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli. Curr Opin Biotechnol 6: 494-500.
    • (1995) Curr Opin Biotechnol , vol.6 , pp. 494-500
    • Kane, J.F.1
  • 12
    • 0033910879 scopus 로고    scopus 로고
    • Continuous refolding of lysozyme with fed-batch addition of denatured protein solution
    • Katoh S, Katoh Y. 2000. Continuous refolding of lysozyme with fed-batch addition of denatured protein solution. Process Biochem 35: 1119-1124.
    • (2000) Process Biochem , vol.35 , pp. 1119-1124
    • Katoh, S.1    Katoh, Y.2
  • 13
    • 0034600953 scopus 로고    scopus 로고
    • BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II
    • Kirsch T, Nickel J, Sebald W. 2000. BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II. EMBO J 19:3314-3324.
    • (2000) EMBO J , vol.19 , pp. 3314-3324
    • Kirsch, T.1    Nickel, J.2    Sebald, W.3
  • 15
    • 0035400037 scopus 로고    scopus 로고
    • Delivering on the promise of bone morphogenetic proteins
    • Li RH, Wozney JM. 2001. Delivering on the promise of bone morphogenetic proteins. Trends Biotechnol 19:255-265.
    • (2001) Trends Biotechnol , vol.19 , pp. 255-265
    • Li, R.H.1    Wozney, J.M.2
  • 16
    • 0031104770 scopus 로고    scopus 로고
    • Effect of inclusion body contaminants on the oxidative renaturation of hen egg white lysozyme
    • Maachupalli-Reddy J, Kelley BD, De Bernardez Clark E. 1997. Effect of inclusion body contaminants on the oxidative renaturation of hen egg white lysozyme. Biotechnol Prog 13:144-150.
    • (1997) Biotechnol Prog , vol.13 , pp. 144-150
    • Maachupalli-Reddy, J.1    Kelley, B.D.2    De Bernardez Clark, E.3
  • 19
    • 0038227075 scopus 로고    scopus 로고
    • Renaturation of heterodimeric platelet-derived growth factor from inclusion bodies of recombinant Escherichia coli using size-exclusion chromatography
    • Müller C, Rinas U. 1999. Renaturation of heterodimeric platelet-derived growth factor from inclusion bodies of recombinant Escherichia coli using size-exclusion chromatography. J Chromatogr A 855:203-213.
    • (1999) J Chromatogr A , vol.855 , pp. 203-213
    • Müller, C.1    Rinas, U.2
  • 20
    • 0034851615 scopus 로고    scopus 로고
    • The pro-sequence facilitates folding of human nerve growth factor from Escherichia coli inclusion bodies
    • Rattenholl A, Lilie H, Grossmann A, Stern A, Schwarz E, Rudolph R. 2001. The pro-sequence facilitates folding of human nerve growth factor from Escherichia coli inclusion bodies. Eur J Biochem 268:3296-3303.
    • (2001) Eur J Biochem , vol.268 , pp. 3296-3303
    • Rattenholl, A.1    Lilie, H.2    Grossmann, A.3    Stern, A.4    Schwarz, E.5    Rudolph, R.6
  • 22
    • 0029985256 scopus 로고    scopus 로고
    • Human bone morphogenetic protein 2 contains a heparin-binding site which modifies its biological activity
    • Ruppert R, Hoffmann E, Sebald W. 1996. Human bone morphogenetic protein 2 contains a heparin-binding site which modifies its biological activity. Eur J Biochem 237:295-302.
    • (1996) Eur J Biochem , vol.237 , pp. 295-302
    • Ruppert, R.1    Hoffmann, E.2    Sebald, W.3
  • 23
    • 0033582942 scopus 로고    scopus 로고
    • Crystal structure of human bone morphogenetic protein-2 at 2.7. Å resolution
    • Scheufler C, Sebald W, Hülsmeyer M. 1999. Crystal structure of human bone morphogenetic protein-2 at 2.7. Å resolution. J Mol Biol 287: 103-115.
    • (1999) J Mol Biol , vol.287 , pp. 103-115
    • Scheufler, C.1    Sebald, W.2    Hülsmeyer, M.3
  • 24
    • 0034966663 scopus 로고    scopus 로고
    • Systematic optimization of expression and refolding of the Plasmodium falciparum cysteine protease Falcipain-2
    • Sijwali PS, Brinen LS, Rosenthal PJ. 2001. Systematic optimization of expression and refolding of the Plasmodium falciparum cysteine protease Falcipain-2. Protein Expr Purif 22:128-134.
    • (2001) Protein Expr Purif , vol.22 , pp. 128-134
    • Sijwali, P.S.1    Brinen, L.S.2    Rosenthal, P.J.3
  • 25
    • 0031688064 scopus 로고    scopus 로고
    • Renaturation of recombinant human neurotrophin-3 from inclusion bodies using an aggregation suppressor
    • Suenaga M, Ohmae H, Tsuji S, Itoh T, Nishimura O. 1998. Renaturation of recombinant human neurotrophin-3 from inclusion bodies using an aggregation suppressor. Biotechnol Appl Biochem 28:119-124.
    • (1998) Biotechnol Appl Biochem , vol.28 , pp. 119-124
    • Suenaga, M.1    Ohmae, H.2    Tsuji, S.3    Itoh, T.4    Nishimura, O.5
  • 26
    • 0030019343 scopus 로고    scopus 로고
    • Effective refolding of fully reduced lysozyme with a flow-type reactor
    • Terashima M, Suzuki K, Katoh S. 1996. Effective refolding of fully reduced lysozyme with a flow-type reactor. Process Biochem 31:341-345.
    • (1996) Process Biochem , vol.31 , pp. 341-345
    • Terashima, M.1    Suzuki, K.2    Katoh, S.3
  • 27
    • 0033152047 scopus 로고    scopus 로고
    • Renaturation of Escherichia coli-derived recombinant human macrophage colony-stimulating factor
    • Tran-Moseman A, Schauer N, De Bernardez Clark E. 1999. Renaturation of Escherichia coli-derived recombinant human macrophage colony-stimulating factor. Protein Expr Purif 16:181-189.
    • (1999) Protein Expr Purif , vol.16 , pp. 181-189
    • Tran-Moseman, A.1    Schauer, N.2    De Bernardez Clark, E.3
  • 29
    • 0041468584 scopus 로고    scopus 로고
    • Strategies for refolding inclusion body proteins
    • Villaverde A, editor. Trivandrum, India: Research Signpost
    • Vallejo LF, Rinas U. 2002. Strategies for refolding inclusion body proteins. In: Villaverde A, editor. Protein production in bacterial cell factories. Trivandrum, India: Research Signpost. p 59-71.
    • (2002) Protein Production in Bacterial Cell Factories , pp. 59-71
    • Vallejo, L.F.1    Rinas, U.2
  • 30
    • 0037187447 scopus 로고    scopus 로고
    • Renaturation and purification of bone morphogenetic protein-2 produced as inclusion bodies in high-cell-density cultures of recombinant Escherichia coli
    • Vallejo LF, Brokelmann M, Marten S, Trappe S, Cabrera-Crespo J, Hoffmann A, Gross G, Weich HA, Rinas U. 2002. Renaturation and purification of bone morphogenetic protein-2 produced as inclusion bodies in high-cell-density cultures of recombinant Escherichia coli. J Biotechnol 94:185-194.
    • (2002) J Biotechnol , vol.94 , pp. 185-194
    • Vallejo, L.F.1    Brokelmann, M.2    Marten, S.3    Trappe, S.4    Cabrera-Crespo, J.5    Hoffmann, A.6    Gross, G.7    Weich, H.A.8    Rinas, U.9
  • 31
    • 1442295783 scopus 로고    scopus 로고
    • Methods of refolding proteins by use of zwitterionic low molecular weight agents. Patent Application WO 99/18196
    • Vicik SM. 1999. Methods of refolding proteins by use of zwitterionic low molecular weight agents. Patent Application WO 99/18196.
    • Vicik, S.M.1
  • 33
    • 77956741418 scopus 로고
    • Ultraviolet spectra of proteins and amino acids
    • Wetlaufer DB. 1962. Ultraviolet spectra of proteins and amino acids. Adv Prot Chem 17:303-390.
    • (1962) Adv Prot Chem , vol.17 , pp. 303-390
    • Wetlaufer, D.B.1
  • 34
    • 0037112617 scopus 로고    scopus 로고
    • Renaturation of human proinsulin - A study on refolding and conversion to insulin
    • Winter J, Lilie H, Rudolph R. 2002. Renaturation of human proinsulin - a study on refolding and conversion to insulin. Anal Biochem 310: 148-155.
    • (2002) Anal Biochem , vol.310 , pp. 148-155
    • Winter, J.1    Lilie, H.2    Rudolph, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.