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Volumn 62, Issue 2, 1998, Pages 143-151

High-level production of human growth hormone in Escherichia coli by a simple recombinant process

Author keywords

Chromatography; Escherichia coli; Human growth hormone

Indexed keywords

AFFINITY CHROMATOGRAPHY; ENZYMES; GENES; HORMONES; ION EXCHANGE; PH EFFECTS; PURIFICATION; SOLUBILITY;

EID: 0344625372     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-1656(98)00054-6     Document Type: Article
Times cited : (47)

References (23)
  • 1
    • 0023629024 scopus 로고
    • Tumor necrosis factors-TNF-α and TNF-β: Their structure and pleiotropic biological effects
    • Aggarwal, B.B., 1987. Tumor necrosis factors-TNF-α and TNF-β: their structure and pleiotropic biological effects. Drugs Future 12, 891-897.
    • (1987) Drugs Future , vol.12 , pp. 891-897
    • Aggarwal, B.B.1
  • 2
    • 0023270946 scopus 로고
    • High-level secretion of human growth hormone by Escherichia coli
    • Chang, N.C., Rey, M., Bochner, B., Heynecker, H., Grey, G., 1987. High-level secretion of human growth hormone by Escherichia coli. Gene 55, 189-196.
    • (1987) Gene , vol.55 , pp. 189-196
    • Chang, N.C.1    Rey, M.2    Bochner, B.3    Heynecker, H.4    Grey, G.5
  • 3
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • De Vos, A.M., Ultsch, M., Kossiakoff, A.A., 1992. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 255, 306-312.
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 4
    • 0023680201 scopus 로고
    • Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein
    • Di Guan, C., Li, P., Riggs, P.D., Inouye, H., 1988. Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein. Gene 67, 21-30.
    • (1988) Gene , vol.67 , pp. 21-30
    • Di Guan, C.1    Li, P.2    Riggs, P.D.3    Inouye, H.4
  • 5
    • 0026058488 scopus 로고
    • A new human growth hormone production process using a recombinant Bacillus subtilis strain
    • Franchi, E., Maisano, F., Testori, S.A., et al., 1991. A new human growth hormone production process using a recombinant Bacillus subtilis strain. J. Biotechnol. 18, 41-54.
    • (1991) J. Biotechnol. , vol.18 , pp. 41-54
    • Franchi, E.1    Maisano, F.2    Testori, S.A.3
  • 6
    • 0022616862 scopus 로고
    • Technology spurt resolves growth hormone problem, ends shortage
    • Glasbrenner, K., 1986. Technology spurt resolves growth hormone problem, ends shortage. J. Am. Med. Assoc. 255, 581-587.
    • (1986) J. Am. Med. Assoc. , vol.255 , pp. 581-587
    • Glasbrenner, K.1
  • 7
    • 0018735990 scopus 로고
    • Direct expression in Escherichia coli of a DNa sequence coding for human growth hormone
    • Goeddel, D.V., Heynecker, H.L., Hozumi, T., et al., 1979. Direct expression in Escherichia coli of a DNA sequence coding for human growth hormone. Nature 281, 544-548.
    • (1979) Nature , vol.281 , pp. 544-548
    • Goeddel, D.V.1    Heynecker, H.L.2    Hozumi, T.3
  • 9
    • 84966159689 scopus 로고
    • High-level expression, efficient secretion and folding of human growth hormone in Escherichia coli
    • Hsiung, H., Mayne, N.G., Becker, G.W., 1986. High-level expression, efficient secretion and folding of human growth hormone in Escherichia coli. Biotechnology 4, 991-995.
    • (1986) Biotechnology , vol.4 , pp. 991-995
    • Hsiung, H.1    Mayne, N.G.2    Becker, G.W.3
  • 10
    • 0023177768 scopus 로고
    • Construction of an excretion vector and extracellular production of human growth hormone from Escherichia coli
    • Kato, C., Kobayashi, T., Kudo, T., et al., 1987. Construction of an excretion vector and extracellular production of human growth hormone from Escherichia coli. Gene 54, 197-202.
    • (1987) Gene , vol.54 , pp. 197-202
    • Kato, C.1    Kobayashi, T.2    Kudo, T.3
  • 11
    • 0029862298 scopus 로고    scopus 로고
    • Production of recombinant human glucagon in Escherichia coli by a novel fusion protein approach
    • Kim, D.-Y., Shin, N.-K., Chang, S.-G., Shin, H.-C., 1996. Production of recombinant human glucagon in Escherichia coli by a novel fusion protein approach. Biotechnol. Tech. 10, 669-672.
    • (1996) Biotechnol. Tech. , vol.10 , pp. 669-672
    • Kim, D.-Y.1    Shin, N.-K.2    Chang, S.-G.3    Shin, H.-C.4
  • 12
    • 0017440456 scopus 로고
    • Growth hormone and the regulation of somatic growth
    • Kostyo, J.L., Isaksson, O., 1977 Growth hormone and the regulation of somatic growth. Int. Rev. Physiol. 13, 255-274.
    • (1977) Int. Rev. Physiol. , vol.13 , pp. 255-274
    • Kostyo, J.L.1    Isaksson, O.2
  • 13
    • 14744292185 scopus 로고
    • A thioredoxin gene fusion expression system that circumvents inclusion body formation in the Escherichia coli cytoplasm
    • La Vallie, E.R., DiBlasio, E.A., Kovacle, S., Grant, K.L., Sohendel, P.F., McCoy, J.M., 1993. A thioredoxin gene fusion expression system that circumvents inclusion body formation in the Escherichia coli cytoplasm. Biotechnology 11, 187-193.
    • (1993) Biotechnology , vol.11 , pp. 187-193
    • La Vallie, E.R.1    Diblasio, E.A.2    Kovacle, S.3    Grant, K.L.4    Sohendel, P.F.5    McCoy, J.M.6
  • 14
    • 0027330977 scopus 로고
    • Enhanced production of α-amylase in fed-batch cultures of Bacillus subtilis TN106[pAT5]
    • Lee, J., Parulekar, S.J., 1993. Enhanced production of α-amylase in fed-batch cultures of Bacillus subtilis TN106[pAT5]. Biotechnol. Bioeng. 42, 1142-1150.
    • (1993) Biotechnol. Bioeng. , vol.42 , pp. 1142-1150
    • Lee, J.1    Parulekar, S.J.2
  • 15
    • 0023186584 scopus 로고
    • Extracellular production of human growth hormone by a head portion of the prepropeptide derived from Bacillus amyloliquefaciens neutral protease in Bacillus subtilis
    • Nakayama, A., Kawamura, K., Shimada, H., Akaoka, A., Mita, J., Honjo, M., Furutani, Y., 1987. Extracellular production of human growth hormone by a head portion of the prepropeptide derived from Bacillus amyloliquefaciens neutral protease in Bacillus subtilis. J. Biotechnol. 5, 171-179.
    • (1987) J. Biotechnol. , vol.5 , pp. 171-179
    • Nakayama, A.1    Kawamura, K.2    Shimada, H.3    Akaoka, A.4    Mita, J.5    Honjo, M.6    Furutani, Y.7
  • 16
    • 0022053837 scopus 로고
    • Immobilization and purification of enzymes with staphylococcal protein a gene fusion vectors
    • Nilsson, B., Abrahmsen, L., Uhlen, M., 1985. Immobilization and purification of enzymes with staphylococcal protein A gene fusion vectors. EMBO J. 4, 1075-1080.
    • (1985) EMBO J. , vol.4 , pp. 1075-1080
    • Nilsson, B.1    Abrahmsen, L.2    Uhlen, M.3
  • 17
    • 0027657324 scopus 로고
    • Structure analysis of continuous cultures subject to periodic medium tuning
    • Parulekar, S.J., Lee, J., 1993. Structure analysis of continuous cultures subject to periodic medium tuning. Chem. Eng. Sci. 48, 3007-3035.
    • (1993) Chem. Eng. Sci. , vol.48 , pp. 3007-3035
    • Parulekar, S.J.1    Lee, J.2
  • 18
    • 0021681058 scopus 로고
    • Human tumor necrosis factor: Precursor structure, expression and homology to lymphotoxin
    • Pennica, D., Nedwin, G.E., Hayflick, J.S., et al., 1984. Human tumor necrosis factor: precursor structure, expression and homology to lymphotoxin. Nature 312, 724-729.
    • (1984) Nature , vol.312 , pp. 724-729
    • Pennica, D.1    Nedwin, G.E.2    Hayflick, J.S.3
  • 19
    • 0343196718 scopus 로고    scopus 로고
    • Enhanced production of human mini-proinsulin in fed-batch cultures at high cell density of Escherichia coli BL21(DE3) [pET-3aT2M2]
    • Shin, C.-S., Hong, M.-S., Bae, C.-S., Lee, J., 1997. Enhanced production of human mini-proinsulin in fed-batch cultures at high cell density of Escherichia coli BL21(DE3) [pET-3aT2M2]. Biotechnol. Prog. 13, 249-257.
    • (1997) Biotechnol. Prog. , vol.13 , pp. 249-257
    • Shin, C.-S.1    Hong, M.-S.2    Bae, C.-S.3    Lee, J.4
  • 22
    • 0021169719 scopus 로고
    • One-step purification of hybrid proteins which have β-galactosidase activity
    • Ulmann, A., 1984. One-step purification of hybrid proteins which have β-galactosidase activity. Gene 29, 27-31.
    • (1984) Gene , vol.29 , pp. 27-31
    • Ulmann, A.1
  • 23
    • 0017095398 scopus 로고
    • Cell surface receptors for insulin and human growth hormone
    • Van Obberghen, E., De Meyts, P., Roth, J., 1976. Cell surface receptors for insulin and human growth hormone. J. Biol. Chem. 251, 6844-6851.
    • (1976) J. Biol. Chem. , vol.251 , pp. 6844-6851
    • Van Obberghen, E.1    De Meyts, P.2    Roth, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.