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Volumn 55, Issue 2, 1997, Pages 101-112

Secretion of authentic 20-kDa human growth hormone (20K hGH) in Escherichia coli and properties of the purified product

Author keywords

20K hGH; Authentic structure; Biological activities; E. coli; Glutathione reductase; Secretion

Indexed keywords

BODY FLUIDS; CELL CULTURE; CHEMICAL MODIFICATION; ENZYME KINETICS; HORMONES; MICROORGANISMS; PROTEINS;

EID: 0343811713     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-1656(97)00062-X     Document Type: Article
Times cited : (49)

References (31)
  • 2
    • 0022473255 scopus 로고
    • Expression, secretion and folding of human growth hormone in Escherichia coli
    • Becker G.W., Hsiung H.M. Expression, secretion and folding of human growth hormone in Escherichia coli. FEBS Lett. 204:1986;145-150.
    • (1986) FEBS Lett. , vol.204 , pp. 145-150
    • Becker, G.W.1    Hsiung, H.M.2
  • 3
    • 0023270946 scopus 로고
    • High-level secretion of human growth hormone by Escherichia coli
    • Chang C.N., Rey M., Bochner B., Heyneker H., Gray G. High-level secretion of human growth hormone by Escherichia coli. Gene. 55:1987;189-196.
    • (1987) Gene , vol.55 , pp. 189-196
    • Chang, C.N.1    Rey, M.2    Bochner, B.3    Heyneker, H.4    Gray, G.5
  • 4
    • 0028299831 scopus 로고
    • Inhibition of growth hormone bioactivity by recombinant human growth hormone-binding protein in the eluted stain assay system
    • Dattani M.T., Hindmarsh P.C., Brook C.G.D., Robinson I.C.A.F., Marshall N.J. Inhibition of growth hormone bioactivity by recombinant human growth hormone-binding protein in the eluted stain assay system. J. Endocrinol. 140:1994;445-453.
    • (1994) J. Endocrinol. , vol.140 , pp. 445-453
    • Dattani, M.T.1    Hindmarsh, P.C.2    Brook, C.G.D.3    Robinson, I.C.A.F.4    Marshall, N.J.5
  • 5
    • 0019785870 scopus 로고
    • Human growth hormone DNA sequence and mRNA structure: Possible alternative splicing
    • DeNoto F.M., Moore D.D., Goodman H.M. Human growth hormone DNA sequence and mRNA structure: possible alternative splicing. Nucleic Acids Res. 9:1981;3719-3730.
    • (1981) Nucleic Acids Res. , vol.9 , pp. 3719-3730
    • Denoto, F.M.1    Moore, D.D.2    Goodman, H.M.3
  • 6
    • 0027739665 scopus 로고
    • Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli
    • Derman A.I., Prinz W.A., Belin D., 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
  • 7
    • 0018615065 scopus 로고
    • The 20,000-dalton structural variant of human growth hormone: Lack of some early insulin-like effects
    • Frigeri L.G., Peterson S.M., Lewis U.J. The 20,000-dalton structural variant of human growth hormone: lack of some early insulin-like effects. Biochem. Biophys. Res. Commun. 91:1979;778-782.
    • (1979) Biochem. Biophys. Res. Commun. , vol.91 , pp. 778-782
    • Frigeri, L.G.1    Peterson, S.M.2    Lewis, U.J.3
  • 8
    • 0022446871 scopus 로고
    • Glutathione reductase from Escherichia coli: Cloning and sequence analysis of the gene and relationship to other flavoprotein disulfide oxidoreductases
    • Greer S., Perham R.N. Glutathione reductase from Escherichia coli: cloning and sequence analysis of the gene and relationship to other flavoprotein disulfide oxidoreductases. Biochemistry. 25:1986;2736-2742.
    • (1986) Biochemistry , vol.25 , pp. 2736-2742
    • Greer, S.1    Perham, R.N.2
  • 9
    • 0026048141 scopus 로고
    • Human growth hormone variant produces insulin-like and lipolytic responses in rat adipose tissue
    • Goodman H.M., Tai L.R., Ray J., Cooke N.E., Liebhaber S.A. Human growth hormone variant produces insulin-like and lipolytic responses in rat adipose tissue. Endocrinology. 129:1991;1779-1783.
    • (1991) Endocrinology , vol.129 , pp. 1779-1783
    • Goodman, H.M.1    Tai, L.R.2    Ray, J.3    Cooke, N.E.4    Liebhaber, S.A.5
  • 10
    • 0015783856 scopus 로고
    • Determination of the amino acid sequence of porcine trypsin by sequenator analysis
    • Hermodson M.A., Ericsson L.H., Neurath H., Walsh K.A. Determination of the amino acid sequence of porcine trypsin by sequenator analysis. Biochemistry. 12:1973;3146-3153.
    • (1973) Biochemistry , vol.12 , pp. 3146-3153
    • Hermodson, M.A.1    Ericsson, L.H.2    Neurath, H.3    Walsh, K.A.4
  • 11
    • 0026701330 scopus 로고
    • Effects of total hydrophobicity and length of the hydrophobic domein of a signal peptide on in vitro translocation efficiency
    • Hikita C., Mizushima S. Effects of total hydrophobicity and length of the hydrophobic domein of a signal peptide on in vitro translocation efficiency. J. Biol. Chem. 267:1992;4882-4888.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4882-4888
    • Hikita, C.1    Mizushima, S.2
  • 12
    • 0026780329 scopus 로고
    • The requirement of a positive charge at the amino terminus can be compensated for by a longer central hydrophobic stretch in the functioning of signal peptide
    • Hikita C., Mizushima S. The requirement of a positive charge at the amino terminus can be compensated for by a longer central hydrophobic stretch in the functioning of signal peptide. J. Biol. Chem. 267:1992;12375-12379.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12375-12379
    • Hikita, C.1    Mizushima, S.2
  • 13
    • 0024222740 scopus 로고
    • Secretion and folding of human growth hormone in Escherichia coli
    • Hsiung H.M., Becker G.W. Secretion and folding of human growth hormone in Escherichia coli. Biotechnol. Genet. Eng. Rev. 6:1988;43-65.
    • (1988) Biotechnol. Genet. Eng. Rev. , vol.6 , pp. 43-65
    • Hsiung, H.M.1    Becker, G.W.2
  • 14
    • 0029618810 scopus 로고
    • 22-kDa and 20-kDa hGH isoforms show differential effects when assayed in 3T3-F443A and 3T3-F442A/C4 adipocytes
    • Juárez-Aguilar E., Castro-Muñozledo F. 22-kDa and 20-kDa hGH isoforms show differential effects when assayed in 3T3-F443A and 3T3-F442A/C4 adipocytes. Biochem. Biophys. Res. Commum. 217:1995;28-33.
    • (1995) Biochem. Biophys. Res. Commum. , vol.217 , pp. 28-33
    • Juárez-Aguilar, E.1    Castro-Muñozledo, F.2
  • 15
    • 0021794499 scopus 로고
    • Biosynthetic 20-kilodalton methionyl-human growth hormone has diabetogenic and insulin-like activities
    • Kostyo J.L., Cameron C.M., Olson K.C., Jones A.J.S., Pai R.C. Biosynthetic 20-kilodalton methionyl-human growth hormone has diabetogenic and insulin-like activities. Proc. Natl. Acad. Sci. USA. 82:1985;4250-4253.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4250-4253
    • Kostyo, J.L.1    Cameron, C.M.2    Olson, K.C.3    Jones, A.J.S.4    Pai, R.C.5
  • 17
    • 0014949207 scopus 로고
    • Cleavage of the structural proteins during assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of the structural proteins during assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0025145822 scopus 로고
    • The 20,000 Da variant of human growth hormone does not bind to growth hormone receptors in human liver
    • McCarter J., Shaw M.A., Winer L.A., Baumann G. The 20,000 Da variant of human growth hormone does not bind to growth hormone receptors in human liver. Mol. Cell. Endocrinol. 73:1990;11-14.
    • (1990) Mol. Cell. Endocrinol. , vol.73 , pp. 11-14
    • McCarter, J.1    Shaw, M.A.2    Winer, L.A.3    Baumann, G.4
  • 19
  • 20
    • 0018844936 scopus 로고
    • Amino acid sequence of the signal peptide of ompA protein, a major outer membrane protein of Escherichia coli
    • Movva N.R., Nakamura K., Inouye M. Amino acid sequence of the signal peptide of ompA protein, a major outer membrane protein of Escherichia coli. J. Biol. Chem. 255:1980;27-29.
    • (1980) J. Biol. Chem. , vol.255 , pp. 27-29
    • Movva, N.R.1    Nakamura, K.2    Inouye, M.3
  • 23
    • 0014010845 scopus 로고
    • The release of enzymes by osmotic shock from Escherichia coli in exponential phase
    • Nossal N.G., Heppel L.A. The release of enzymes by osmotic shock from Escherichia coli in exponential phase. J. Biol. Chem. 241:1966;3055-3062.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3055-3062
    • Nossal, N.G.1    Heppel, L.A.2
  • 25
    • 0023883241 scopus 로고
    • Sequence of thioredoxin reductase from Escherichia coli: Relationship to other flavoprotein disulfide oxidoreductases
    • Russel M., Model P. Sequence of thioredoxin reductase from Escherichia coli: relationship to other flavoprotein disulfide oxidoreductases. J. Biol. Chem. 263:1988;9015-9019.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9015-9019
    • Russel, M.1    Model, P.2
  • 26
    • 0023655884 scopus 로고
    • Receptor binding properties and insulin-like effects of human growth hormone and its 20 kDa-variant in rat adipocytes
    • Smal J., Closset J., Hennen G., De Meyts P. Receptor binding properties and insulin-like effects of human growth hormone and its 20 kDa-variant in rat adipocytes. J. Biol. Chem. 262:1987;11071-11079.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11071-11079
    • Smal, J.1    Closset, J.2    Hennen, G.3    De Meyts, P.4
  • 27
    • 0028983021 scopus 로고
    • β-Galactosidase is inactivated by intermolecular disulfide bonds and is toxic when secreted to the periplasm of Escherichia coli
    • Snyder W.B., Silhavy T.J. β-Galactosidase is inactivated by intermolecular disulfide bonds and is toxic when secreted to the periplasm of Escherichia coli. J. Bacteriol. 177:1995;953-963.
    • (1995) J. Bacteriol. , vol.177 , pp. 953-963
    • Snyder, W.B.1    Silhavy, T.J.2
  • 28
    • 0028032203 scopus 로고
    • The X-ray structure of a growth hormone-prolactin receptor complex
    • Sommers W., Ultsch M., De Vos A.M., Kossiakoff A.A. The X-ray structure of a growth hormone-prolactin receptor complex. Nature. 372:1994;478-481.
    • (1994) Nature , vol.372 , pp. 478-481
    • Sommers, W.1    Ultsch, M.2    De Vos, A.M.3    Kossiakoff, A.A.4
  • 29
    • 0019169639 scopus 로고
    • A new sensitive and specific bioassay for lactogenic hormones: Measurement of prolactin and growth hormone in human serum
    • Tanaka T., Shiu R.P.C., Gout P.W., Beer C.T., Nobel R.T., Friesen H.G. A new sensitive and specific bioassay for lactogenic hormones: measurement of prolactin and growth hormone in human serum. J. Clin. Endocrinol. Metab. 51:1980;1058-1063.
    • (1980) J. Clin. Endocrinol. Metab. , vol.51 , pp. 1058-1063
    • Tanaka, T.1    Shiu, R.P.C.2    Gout, P.W.3    Beer, C.T.4    Nobel, R.T.5    Friesen, H.G.6
  • 30
    • 0017165455 scopus 로고
    • Glutathione reductase from human erythrocytes
    • Worthington D.J., Rosemeyer M.A. Glutathione reductase from human erythrocytes. Eur. J. Biochem. 67:1976;231-238.
    • (1976) Eur. J. Biochem. , vol.67 , pp. 231-238
    • Worthington, D.J.1    Rosemeyer, M.A.2
  • 31
    • 0019386665 scopus 로고
    • Nucleotide sequence coding for the respiratory NADH dehydrogenase of Escherichia coli
    • Young J.G., Rogers B.L., Campbell H.D., Jaworowski A., Shaw D.C. Nucleotide sequence coding for the respiratory NADH dehydrogenase of Escherichia coli. Eur. J. Biochem. 116:1981;165-170.
    • (1981) Eur. J. Biochem. , vol.116 , pp. 165-170
    • Young, J.G.1    Rogers, B.L.2    Campbell, H.D.3    Jaworowski, A.4    Shaw, D.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.