메뉴 건너뛰기




Volumn 60, Issue 1, 2008, Pages 7-14

Recombinant human epidermal growth factor inclusion body solubilization and refolding at large scale using expanded-bed adsorption chromatography from Escherichia coli

Author keywords

Escherichia coli fermentation; Expanded bed adsorption (EBA); Physiochemical characterization; Protein purification; Recombinant human epidermal growth factor (rhEGF); Scale up

Indexed keywords

EPIDERMAL GROWTH FACTOR; RECOMBINANT PROTEIN;

EID: 43749103118     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2008.02.020     Document Type: Article
Times cited : (22)

References (30)
  • 1
    • 84916265276 scopus 로고
    • Isolation of a mouse submaxillary gland protein accelerating incisor eruption and eyelid opening in the new-born animal
    • Cohen S. Isolation of a mouse submaxillary gland protein accelerating incisor eruption and eyelid opening in the new-born animal. J. Biol. Chem. 237 (1962) 1555-1562
    • (1962) J. Biol. Chem. , vol.237 , pp. 1555-1562
    • Cohen, S.1
  • 2
    • 0028954548 scopus 로고
    • Epidermal growth factor-related peptides and their relevance to gastrointestinal pathophysiology
    • Barnard J.A., Beauchamp R.D., Russell W.E., Dubois R.N., and Coffey R.J. Epidermal growth factor-related peptides and their relevance to gastrointestinal pathophysiology. Gastroenterology 108 (1995) 564-580
    • (1995) Gastroenterology , vol.108 , pp. 564-580
    • Barnard, J.A.1    Beauchamp, R.D.2    Russell, W.E.3    Dubois, R.N.4    Coffey, R.J.5
  • 3
    • 0029883668 scopus 로고    scopus 로고
    • Why is epidermal growth factor present in the gut lumen?
    • Playford R.J., and Wright N.A. Why is epidermal growth factor present in the gut lumen?. Gut 38 (1996) 303-305
    • (1996) Gut , vol.38 , pp. 303-305
    • Playford, R.J.1    Wright, N.A.2
  • 5
    • 0025208268 scopus 로고
    • Effects of epidermal growth factor on bone formation and resorption in vivo
    • Marie P.J., Hott M., and Perheentupa J. Effects of epidermal growth factor on bone formation and resorption in vivo. Am. J. Physiol. Endocrinol. Metab. 258 (1990) E275-E281
    • (1990) Am. J. Physiol. Endocrinol. Metab. , vol.258
    • Marie, P.J.1    Hott, M.2    Perheentupa, J.3
  • 6
    • 0000686740 scopus 로고
    • Human epidermal growth factor: isolation and chemical and biological properties
    • Cohen S., and Carpenter G. Human epidermal growth factor: isolation and chemical and biological properties. PNAS 72 (1975) 1317-1321
    • (1975) PNAS , vol.72 , pp. 1317-1321
    • Cohen, S.1    Carpenter, G.2
  • 7
    • 0016698196 scopus 로고
    • Epidermal growth factor: identification of a new hormone in human urine
    • Starkey R.H., Cohen S., and Orth D.N. Epidermal growth factor: identification of a new hormone in human urine. Science 189 (1975) 800-802
    • (1975) Science , vol.189 , pp. 800-802
    • Starkey, R.H.1    Cohen, S.2    Orth, D.N.3
  • 8
    • 0016719486 scopus 로고
    • Isolation and structure of urogastrone and its relationship to epidermal growth factor
    • Gregory H. Isolation and structure of urogastrone and its relationship to epidermal growth factor. Nature 257 (1975) 325-327
    • (1975) Nature , vol.257 , pp. 325-327
    • Gregory, H.1
  • 9
    • 0016834989 scopus 로고
    • The isolation of the urogastrone inhibitors of gastric acid secretion from human urine
    • Gregory H., and Willshire I.R. The isolation of the urogastrone inhibitors of gastric acid secretion from human urine. Physiol. Chem. 356 (1975) 1765-1774
    • (1975) Physiol. Chem. , vol.356 , pp. 1765-1774
    • Gregory, H.1    Willshire, I.R.2
  • 10
    • 0042090308 scopus 로고    scopus 로고
    • Purification of soluble human epidermal growth factor (hEGF) from recombinant Escherichia coli culture broth by using expanded-bed adsorption chromatography
    • Lee Y.S., Suh C.W., Park S.K., and Lee E.K. Purification of soluble human epidermal growth factor (hEGF) from recombinant Escherichia coli culture broth by using expanded-bed adsorption chromatography. Biotechnol. Appl. Biochem. 38 (2003) 9-13
    • (2003) Biotechnol. Appl. Biochem. , vol.38 , pp. 9-13
    • Lee, Y.S.1    Suh, C.W.2    Park, S.K.3    Lee, E.K.4
  • 11
    • 38349138998 scopus 로고    scopus 로고
    • Renaturation, purification and characterization of streptokinase expressed as inclusion body in recombinant E. coli
    • Cherish Babu P.V., Srinivas V.K., Mohan V.K., and Krishna E. Renaturation, purification and characterization of streptokinase expressed as inclusion body in recombinant E. coli. J. Chromatogr. B 861 (2007) 218-226
    • (2007) J. Chromatogr. B , vol.861 , pp. 218-226
    • Cherish Babu, P.V.1    Srinivas, V.K.2    Mohan, V.K.3    Krishna, E.4
  • 12
    • 33748126248 scopus 로고    scopus 로고
    • The refolding of different α-fetoprotein variants
    • Leong S.J.S., and Middelberg P.J.A. The refolding of different α-fetoprotein variants. Protein Sci. 15 (2006) 2040-2050
    • (2006) Protein Sci. , vol.15 , pp. 2040-2050
    • Leong, S.J.S.1    Middelberg, P.J.A.2
  • 13
    • 17144364275 scopus 로고    scopus 로고
    • Catalysis of creatine kinase refolding by protein disulfide isomerase involves disulfide cross-link and dimer to tetramer switch
    • Zhao T.J., Ou W.B., Xie Q., Liu Y., Yan Y.B., and Zhou H.M. Catalysis of creatine kinase refolding by protein disulfide isomerase involves disulfide cross-link and dimer to tetramer switch. J. Biol. Chem. 280 (2005) 13470-13476
    • (2005) J. Biol. Chem. , vol.280 , pp. 13470-13476
    • Zhao, T.J.1    Ou, W.B.2    Xie, Q.3    Liu, Y.4    Yan, Y.B.5    Zhou, H.M.6
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0022499115 scopus 로고
    • Large scale high-performance liquid chromatography of urogastrone produced by recombinant DNA technology
    • Brewer S.J., Dickerson C.H., Ewbank J., and Fallon A. Large scale high-performance liquid chromatography of urogastrone produced by recombinant DNA technology. J. Chromatogr. 362 (1986) 443-449
    • (1986) J. Chromatogr. , vol.362 , pp. 443-449
    • Brewer, S.J.1    Dickerson, C.H.2    Ewbank, J.3    Fallon, A.4
  • 16
    • 0023713027 scopus 로고
    • Expression of human epidermal growth factor precursor cDNA in transfected mouse NIH 3T3 cells
    • Mroczkowski B., Reich M., Whittaker J., Bell G.I., and Cohen S. Expression of human epidermal growth factor precursor cDNA in transfected mouse NIH 3T3 cells. Proc. Natl. Acad. Sci. 85 (1988) 126-130
    • (1988) Proc. Natl. Acad. Sci. , vol.85 , pp. 126-130
    • Mroczkowski, B.1    Reich, M.2    Whittaker, J.3    Bell, G.I.4    Cohen, S.5
  • 17
    • 0024316391 scopus 로고
    • Recombinant human epidermal growth factor precursor is a glycosylated membrane protein with biological activity
    • Mroczkowski B., Reich M., Chen K., Bell G.I., and Cohen S. Recombinant human epidermal growth factor precursor is a glycosylated membrane protein with biological activity. Mol. Cell. Biol. 9 (1989) 2771-2778
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2771-2778
    • Mroczkowski, B.1    Reich, M.2    Chen, K.3    Bell, G.I.4    Cohen, S.5
  • 18
    • 0034105491 scopus 로고    scopus 로고
    • Optimization of inclusion body solubilization and renaturation of recombinant human growth hormone from Escherichia coli
    • Patra A.K., Mukhopadhyay R., Mukhija R., Krishnan A., Garg L.C., and Panda A.K. Optimization of inclusion body solubilization and renaturation of recombinant human growth hormone from Escherichia coli. Protein Expr. Purif. 18 (2000) 182-192
    • (2000) Protein Expr. Purif. , vol.18 , pp. 182-192
    • Patra, A.K.1    Mukhopadhyay, R.2    Mukhija, R.3    Krishnan, A.4    Garg, L.C.5    Panda, A.K.6
  • 19
    • 0021736823 scopus 로고
    • Chemical synthesis and cloning of a poly(arginine)-coding gene fragment designed to aid polypeptide purification
    • Smith J.C., Derbyshire R.B., Cook E., Dunthorne L., Viney J., Brewer S.J., Sassenfeld H.M., and Bell L.D. Chemical synthesis and cloning of a poly(arginine)-coding gene fragment designed to aid polypeptide purification. Gene 32 (1984) 321-327
    • (1984) Gene , vol.32 , pp. 321-327
    • Smith, J.C.1    Derbyshire, R.B.2    Cook, E.3    Dunthorne, L.4    Viney, J.5    Brewer, S.J.6    Sassenfeld, H.M.7    Bell, L.D.8
  • 20
    • 0021320171 scopus 로고
    • Polypeptide fusion designed for the purification of recombinant proteins
    • Sassenfeld H.M., and Brewer S.J. Polypeptide fusion designed for the purification of recombinant proteins. Bio/Technology 2 (1984) 76-81
    • (1984) Bio/Technology , vol.2 , pp. 76-81
    • Sassenfeld, H.M.1    Brewer, S.J.2
  • 21
    • 0021889707 scopus 로고
    • The purification of recombinant proteins using C-terminal polyarginine fusions
    • Brewer S.J., and Sassenfeld J.M. The purification of recombinant proteins using C-terminal polyarginine fusions. Trends Biotechnol. 3 (1985) 119-122
    • (1985) Trends Biotechnol. , vol.3 , pp. 119-122
    • Brewer, S.J.1    Sassenfeld, J.M.2
  • 22
    • 23044476987 scopus 로고    scopus 로고
    • Genetically engineered horseradish peroxidase for facilitated purification from baculovirus cultures by cation-exchange chromatography
    • Levin G., Mendive F., Targovnik H.M., Cascone O., and Miranda M.V. Genetically engineered horseradish peroxidase for facilitated purification from baculovirus cultures by cation-exchange chromatography. J. Biotechnol. 118 (2005) 363-369
    • (2005) J. Biotechnol. , vol.118 , pp. 363-369
    • Levin, G.1    Mendive, F.2    Targovnik, H.M.3    Cascone, O.4    Miranda, M.V.5
  • 23
    • 33646779162 scopus 로고    scopus 로고
    • Application of poly-arginine fused minichaperone to renaturation of cyclodextrin glycosyltransferase expressed in recombinant Escherichia coli
    • Kim S.G., Kim J.A., Yu H.A., Lee D.H., Kweon D.H., and Seo J.H. Application of poly-arginine fused minichaperone to renaturation of cyclodextrin glycosyltransferase expressed in recombinant Escherichia coli. Enzyme Microb. Technol. 39 (2006) 459-465
    • (2006) Enzyme Microb. Technol. , vol.39 , pp. 459-465
    • Kim, S.G.1    Kim, J.A.2    Yu, H.A.3    Lee, D.H.4    Kweon, D.H.5    Seo, J.H.6
  • 24
    • 24744466678 scopus 로고    scopus 로고
    • Improved recovery of a fusion protein containing the antigenic domain 1 of the human cytomegalovirus glycoprotein B
    • Ferreira S., Sousa F., Queiroz J.A., and Domingues F.C. Improved recovery of a fusion protein containing the antigenic domain 1 of the human cytomegalovirus glycoprotein B. Biotechnol. Lett. 27 (2005) 1241-1245
    • (2005) Biotechnol. Lett. , vol.27 , pp. 1241-1245
    • Ferreira, S.1    Sousa, F.2    Queiroz, J.A.3    Domingues, F.C.4
  • 25
    • 33947394785 scopus 로고    scopus 로고
    • Expression, purification, and characterization of recombinant human interleukin 24 in Escherichia coli
    • Yang J., Zhang W., Liu K., Jing S., Guo G., Luo P., and Zou Q. Expression, purification, and characterization of recombinant human interleukin 24 in Escherichia coli. Protein Expr. Purif. 53 (2007) 339-345
    • (2007) Protein Expr. Purif. , vol.53 , pp. 339-345
    • Yang, J.1    Zhang, W.2    Liu, K.3    Jing, S.4    Guo, G.5    Luo, P.6    Zou, Q.7
  • 26
    • 0345643118 scopus 로고
    • Rapid purification and partial characterization of recombinant human epidermal growth factor produced by Escherichia coli
    • Yadwad V.B., Meghji K., and Ward O.P. Rapid purification and partial characterization of recombinant human epidermal growth factor produced by Escherichia coli. Biotechnol. Tech. 7 (1993) 657-662
    • (1993) Biotechnol. Tech. , vol.7 , pp. 657-662
    • Yadwad, V.B.1    Meghji, K.2    Ward, O.P.3
  • 27
    • 0346108604 scopus 로고    scopus 로고
    • Scale-up process for expression and renaturation of recombinant human epidermal growth factor from Escherichia coli inclusion bodies
    • Lee J.Y., Yoon C.S., Chung Y., Lee Y.S., and Lee E.K. Scale-up process for expression and renaturation of recombinant human epidermal growth factor from Escherichia coli inclusion bodies. Biotechnol. Appl. Biochem. 31 (2000) 245-248
    • (2000) Biotechnol. Appl. Biochem. , vol.31 , pp. 245-248
    • Lee, J.Y.1    Yoon, C.S.2    Chung, Y.3    Lee, Y.S.4    Lee, E.K.5
  • 28
    • 12944261956 scopus 로고    scopus 로고
    • Partial purification properties of human epidermal growth factor from recombinant Escherichia coli by expanded bed adsorption
    • Tong W.Y., Yao S.J., and Zhu Z.Q. Partial purification properties of human epidermal growth factor from recombinant Escherichia coli by expanded bed adsorption. World J. Microbiol. Biotechnol. 21 (2005) 51-57
    • (2005) World J. Microbiol. Biotechnol. , vol.21 , pp. 51-57
    • Tong, W.Y.1    Yao, S.J.2    Zhu, Z.Q.3
  • 29
    • 33748338753 scopus 로고    scopus 로고
    • A phase III study to evaluate the safety and efficacy of recombinant human epidermal growth factor (REGEN-D™ 150) in healing diabetic foot ulcers
    • Viswanathan V., Pendsey S., Sekar N., and Murthy G.S.R. A phase III study to evaluate the safety and efficacy of recombinant human epidermal growth factor (REGEN-D™ 150) in healing diabetic foot ulcers. Wounds 18 (2006) 186-196
    • (2006) Wounds , vol.18 , pp. 186-196
    • Viswanathan, V.1    Pendsey, S.2    Sekar, N.3    Murthy, G.S.R.4
  • 30
    • 35748972337 scopus 로고    scopus 로고
    • Recombinant human epidermal growth factor (REGEN-D™ 150): effect on healing of diabetic foot ulcers
    • Mohan V.K. Recombinant human epidermal growth factor (REGEN-D™ 150): effect on healing of diabetic foot ulcers. Diabetes Res. Clin. Pract. 78 (2007) 405-411
    • (2007) Diabetes Res. Clin. Pract. , vol.78 , pp. 405-411
    • Mohan, V.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.