메뉴 건너뛰기




Volumn 11, Issue 2, 1997, Pages 169-178

Refolding of a recombinant collagen-targeted TGF-β2 fusion protein expressed in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; MUSTELA VISON;

EID: 0031282125     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1997.0784     Document Type: Article
Times cited : (32)

References (32)
  • 1
    • 0025222517 scopus 로고
    • The transforming growth factor-β family
    • Massague J. The transforming growth factor-β family. Annu. Rev. Cell Biol. 6:1990;597-641.
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 597-641
    • Massague, J.1
  • 3
    • 0000116653 scopus 로고
    • The transforming growth factor-βs, peptide growth factors and their receptors I
    • Roberts A. B., Sporn M. B. The transforming growth factor-βs, peptide growth factors and their receptors I. Handbook Exp. Pharmacol. 95:1990;419-472.
    • (1990) Handbook Exp. Pharmacol. , vol.95 , pp. 419-472
    • Roberts, A.B.1    Sporn, M.B.2
  • 4
    • 0024816337 scopus 로고
    • Human transforming growth factor-beta-3: Recombinant expression, purification, and biological activities in comparison with transforming growth factor-beta 1 and -beta 2
    • Graycar J. L., Miller D. A., Arrick B. A., Lyons R. M., Moses H. L., Derynck R. Human transforming growth factor-beta-3: Recombinant expression, purification, and biological activities in comparison with transforming growth factor-beta 1 and -beta 2. Mol. Endo. 3:1989;1977-1986.
    • (1989) Mol. Endo. , vol.3 , pp. 1977-1986
    • Graycar, J.L.1    Miller, D.A.2    Arrick, B.A.3    Lyons, R.M.4    Moses, H.L.5    Derynck, R.6
  • 5
    • 0026747854 scopus 로고
    • Identification of a structural domain that distinguish the action of the type 1 and 2 isoforms of transforming growth factor beta on endothelial cells
    • Qian S. W., Burmester J. K., Merwin J. R., Madri J. A., Sporn M. B., Roberts A. B. Identification of a structural domain that distinguish the action of the type 1 and 2 isoforms of transforming growth factor beta on endothelial cells. Proc. Natl. Acad. Sci. USA. 89:1992;6290-6294.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6290-6294
    • Qian, S.W.1    Burmester, J.K.2    Merwin, J.R.3    Madri, J.A.4    Sporn, M.B.5    Roberts, A.B.6
  • 7
    • 0027584067 scopus 로고
    • Recombinant human transforming growth factor-β2: Expression by Chinese hamster ovary cells, isolation, and characterization
    • Bourdrel L., Lin C. H., Lauren S. L., Elmore R. H., Sugarman B. J., Hu S., Westcoot K. R. Recombinant human transforming growth factor-β2: Expression by Chinese hamster ovary cells, isolation, and characterization. Protein. Express. Purif. 4:1993;130-140.
    • (1993) Protein. Express. Purif. , vol.4 , pp. 130-140
    • Bourdrel, L.1    Lin, C.H.2    Lauren, S.L.3    Elmore, R.H.4    Sugarman, B.J.5    Hu, S.6    Westcoot, K.R.7
  • 8
    • 0020036666 scopus 로고
    • Cytoplasmic inclusion bodies in Escherichia coli producing biosynthetic human insulin proteins
    • Williams D. C., Van-Frank R. M., Muth W. L., Burnett J. P. Cytoplasmic inclusion bodies in Escherichia coli producing biosynthetic human insulin proteins. Science. 215:1982;687-689.
    • (1982) Science , vol.215 , pp. 687-689
    • Williams, D.C.1    Van-Frank, R.M.2    Muth, W.L.3    Burnett, J.P.4
  • 9
    • 0027122245 scopus 로고
    • Crsytal structure of transforming growth factor-β2: An unusual fold for the superfamily
    • Sun D., Piez K. A., Ogawa Y., Daviers D. R. Crsytal structure of transforming growth factor-β2: an unusual fold for the superfamily. Science. 257:1992;369-373.
    • (1992) Science , vol.257 , pp. 369-373
    • Sun, D.1    Piez, K.A.2    Ogawa, Y.3    Daviers, D.R.4
  • 10
    • 0026633842 scopus 로고
    • An unusual feature revealed by the crystal structure at 2.2Å resolution of human transforming growth factor-beta 2
    • Schlunegger M. P., Grutter M. G. An unusual feature revealed by the crystal structure at 2.2Å resolution of human transforming growth factor-beta 2. Nature. 358:1992;430-434.
    • (1992) Nature , vol.358 , pp. 430-434
    • Schlunegger, M.P.1    Grutter, M.G.2
  • 11
    • 0016411482 scopus 로고
    • Experimental and theoretical aspects of protein folding
    • San Diego: Academic Press. p. 205-299
    • Anfisen C. B., Scheraga H. A. Experimental and theoretical aspects of protein folding. Advances on Protein Chemistry. 1975;Academic Press, San Diego. p. 205-299.
    • (1975) Advances on Protein Chemistry
    • Anfisen, C.B.1    Scheraga, H.A.2
  • 12
    • 0026737319 scopus 로고
    • A collagen/gelatin binding decapeptide derived from bovine peopolypeptide of von Willebrand factor
    • Takagi J., Asai H., Satio Y. A collagen/gelatin binding decapeptide derived from bovine peopolypeptide of von Willebrand factor. Biochemistry. 31:1992;8530-8534.
    • (1992) Biochemistry , vol.31 , pp. 8530-8534
    • Takagi, J.1    Asai, H.2    Satio, Y.3
  • 13
    • 0020479426 scopus 로고
    • Cytoplasmic dot hybridization: Simple analysis relative mRNA levels in multiple small cell or tissue samples
    • White B. A., Bancroft F. C. Cytoplasmic dot hybridization: Simple analysis relative mRNA levels in multiple small cell or tissue samples. J. Bio. Chem. 257:1982;8569-8572.
    • (1982) J. Bio. Chem. , vol.257 , pp. 8569-8572
    • White, B.A.1    Bancroft, F.C.2
  • 15
    • 0028328817 scopus 로고
    • An assay for transforming growth factor-beta using cells transfected with a plasminogen activator inhibitor-1 promoter-luciferase construct
    • Abe M., Harpel J. G., Metz C. N., Nunes I., Loskutoff D. J., Rifkin D. B. An assay for transforming growth factor-beta using cells transfected with a plasminogen activator inhibitor-1 promoter-luciferase construct. Anal. Biol. 216:1994;276-284.
    • (1994) Anal. Biol. , vol.216 , pp. 276-284
    • Abe, M.1    Harpel, J.G.2    Metz, C.N.3    Nunes, I.4    Loskutoff, D.J.5    Rifkin, D.B.6
  • 17
    • 0019215155 scopus 로고
    • The molecular organization of collagen and its role in determining the biological properties of the connective tissue
    • Nimni M. The molecular organization of collagen and its role in determining the biological properties of the connective tissue. Biorheology. 17:1980;51-82.
    • (1980) Biorheology , vol.17 , pp. 51-82
    • Nimni, M.1
  • 18
    • 0028034273 scopus 로고
    • Effects of redox environment on the in vitro folding of RTEM-1 b-lactamase and Escherichia coli alkaline phosphatase
    • Walker K. W., Gilbert H. F. Effects of redox environment on the in vitro folding of RTEM-1 b-lactamase and Escherichia coli alkaline phosphatase. J. Biol. Chem. 269:1994;28487-28493.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28487-28493
    • Walker, K.W.1    Gilbert, H.F.2
  • 19
    • 0030046574 scopus 로고    scopus 로고
    • In vitro folding of inclusion body proteins
    • de Gruyter W., Rudolph R., Lilie H. In vitro folding of inclusion body proteins. FASEB J. 10:1996;49-56.
    • (1996) FASEB J. , vol.10 , pp. 49-56
    • De Gruyter, W.1    Rudolph, R.2    Lilie, H.3
  • 20
    • 0028036622 scopus 로고
    • Intracellular trapping of a cytoplasmic folding intermediates of the phage P22 tailpike using iodoacetamide
    • Sather S. K., King J. Intracellular trapping of a cytoplasmic folding intermediates of the phage P22 tailpike using iodoacetamide. J. Biol. Chem. 269:1994;25268-25276.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25268-25276
    • Sather, S.K.1    King, J.2
  • 21
    • 0039692692 scopus 로고
    • Mechanism of inclusion body formation
    • Washington: American Chemical Society. p. 35-49
    • Mitraki A., Haase, Pettingell C., King J. Mechanism of inclusion body formation. Protein Refolding. 1991;American Chemical Society, Washington. p. 35-49.
    • (1991) Protein Refolding
    • Mitraki, A.1    Haase2    Pettingell, C.3    King, J.4
  • 22
    • 0029001489 scopus 로고
    • Comparing the refolding and reoxidation of recombinant porcine growth hormone from a urea denatured state and from Escherichia coli inclusion bodies
    • Cardamone M., Puri N. K., Brandon M. R. Comparing the refolding and reoxidation of recombinant porcine growth hormone from a urea denatured state and from Escherichia coli inclusion bodies. Biochemistry. 34:1995;5773-5794.
    • (1995) Biochemistry , vol.34 , pp. 5773-5794
    • Cardamone, M.1    Puri, N.K.2    Brandon, M.R.3
  • 23
    • 0027645339 scopus 로고
    • High yields of active STb enterotoxin from a fusion protein (MBP-STb) expression in Escherichia coli
    • Hasndl C. E., Harel J., Flock J. I., Dubreuil J. D. High yields of active STb enterotoxin from a fusion protein (MBP-STb) expression in Escherichia coli. Prot. Express. Purif. 4:1993;275-281.
    • (1993) Prot. Express. Purif. , vol.4 , pp. 275-281
    • Hasndl, C.E.1    Harel, J.2    Flock, J.I.3    Dubreuil, J.D.4
  • 24
    • 0026770746 scopus 로고
    • Polyethylene glycol enhanced refolding of bovine carbonic anhydrase
    • Cleland J., Hedgepeth C., Wang D. Polyethylene glycol enhanced refolding of bovine carbonic anhydrase. J. Biol. Chem. 267:1992;13327-13334.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13327-13334
    • Cleland, J.1    Hedgepeth, C.2    Wang, D.3
  • 25
    • 85030301672 scopus 로고
    • Active reactive kinase refolding from inclusion bosies in E. coli: Improved recovery by removal of contaminating protease
    • Washington: American Chemical Society. p. 153-168
    • Babbitt P. C., West B., Buechter D., Chen L., Kuntz I. D., Kenyon G. Active reactive kinase refolding from inclusion bosies in E. coli: Improved recovery by removal of contaminating protease. Protein Refolding. 1991;American Chemical Society, Washington. p. 153-168.
    • (1991) Protein Refolding
    • Babbitt, P.C.1    West, B.2    Buechter, D.3    Chen, L.4    Kuntz, I.D.5    Kenyon, G.6
  • 27
    • 0025373853 scopus 로고
    • Requirement for activin A and transforming growth factor-beta1 pro-regions in homodimer assembly
    • Gary A. M., Mason A. J. Requirement for activin A and transforming growth factor-beta1 pro-regions in homodimer assembly. Science. 247:1990;1328-1330.
    • (1990) Science , vol.247 , pp. 1328-1330
    • Gary, A.M.1    Mason, A.J.2
  • 28
    • 0026778310 scopus 로고
    • Transforming growth factor-β In disease: The dark side of tissue repair
    • Border W. A., Ruoslahti E. Transforming growth factor-β in disease: the dark side of tissue repair. J. Clin. Invest. 90:1992;1-7.
    • (1992) J. Clin. Invest. , vol.90 , pp. 1-7
    • Border, W.A.1    Ruoslahti, E.2
  • 29
    • 0027976511 scopus 로고
    • Betaglycan can act as a dual modulator of TGF-β access to signaling receptor: Mapping of ligand bonding and GAG attachment sites
    • Lopez C. F., Payne H. M., Andres J. L., Massague J. Betaglycan can act as a dual modulator of TGF-β access to signaling receptor: Mapping of ligand bonding and GAG attachment sites. J. Cell Biol. 124:1994;557-568.
    • (1994) J. Cell Biol. , vol.124 , pp. 557-568
    • Lopez, C.F.1    Payne, H.M.2    Andres, J.L.3    Massague, J.4
  • 30
    • 0026080765 scopus 로고
    • Proteoglycans as modulators of growth factor activities
    • Ruoalahti E., Yamaguchi Y. Proteoglycans as modulators of growth factor activities. Cell. 64:1991;867-869.
    • (1991) Cell , vol.64 , pp. 867-869
    • Ruoalahti, E.1    Yamaguchi, Y.2
  • 31
    • 0027976521 scopus 로고
    • Latent transforming growth factor-β1 associates to fibroblast extracellular matrix via latent TGF-β binding protein
    • Taipale J., Miyazono K., Hekdin C., Keski O. J. latent transforming growth factor-β1 associates to fibroblast extracellular matrix via latent TGF-β binding protein. J. Cell Biol. 124:1994;171-181.
    • (1994) J. Cell Biol. , vol.124 , pp. 171-181
    • Taipale, J.1    Miyazono, K.2    Hekdin, C.3    Keski, O.J.4
  • 32
    • 0027321319 scopus 로고
    • A 60 kD mediates the binding of transforming growth factor-β To cell surface and extracellular matrix proteoglycans
    • Butzow R., Fukushima C., Twardzik D. R., Ruoslahti E. A 60 kD mediates the binding of transforming growth factor-β to cell surface and extracellular matrix proteoglycans. J. Cell Biol. 122:1993;721-727.
    • (1993) J. Cell Biol. , vol.122 , pp. 721-727
    • Butzow, R.1    Fukushima, C.2    Twardzik, D.R.3    Ruoslahti, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.