메뉴 건너뛰기




Volumn 57, Issue 5, 1998, Pages 600-609

Enhanced secretion of human granulocyte colony-stimulating factor directed by a novel hybrid fusion peptide from recombinant Saccharomyces cerevisiae at high cell concentration

Author keywords

Conformation; Fusion protein; Glycosylation; Multimer; RhG CSF; Secretion efficiency

Indexed keywords

AMINO ACIDS; BATCH CELL CULTURE; BIOSYNTHESIS; CELL MEMBRANES; COMPOSITION EFFECTS; CONFORMATIONS; PROTEINS; SURFACE ACTIVE AGENTS; YEAST;

EID: 0344605531     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19980305)57:5<600::AID-BIT12>3.0.CO;2-F     Document Type: Article
Times cited : (32)

References (30)
  • 1
    • 0027138673 scopus 로고
    • Cysteine 17 of recombinant human granulocyte colony- Stimulating factor is partially solvent-exposed
    • Arakawa, T., Prestrelski, S. J., Narhi, L. O., Boone, T. C., Kenney, W. C. 1993. Cysteine 17 of recombinant human granulocyte colony- stimulating factor is partially solvent-exposed. J. Protein Chem. 12 (5): 525-531.
    • (1993) J. Protein Chem. , vol.12 , Issue.5 , pp. 525-531
    • Arakawa, T.1    Prestrelski, S.J.2    Narhi, L.O.3    Boone, T.C.4    Kenney, W.C.5
  • 2
    • 0023061489 scopus 로고
    • A novel leader peptide which allows efficient secretion of a fragment of human interleukin 1β in Saccharomyces cerevisiae
    • Baldari, C., Murray, J. A. H., Ghiara, P., Cesareni, G., Galeotti, C. L. 1987. A novel leader peptide which allows efficient secretion of a fragment of human interleukin 1β in Saccharomyces cerevisiae. EMBO J. 6 (1): 229-234.
    • (1987) EMBO J. , vol.6 , Issue.1 , pp. 229-234
    • Baldari, C.1    Murray, J.A.H.2    Ghiara, P.3    Cesareni, G.4    Galeotti, C.L.5
  • 3
    • 0025774743 scopus 로고
    • The large surface protein of hepatitis B virus is retained in the yeast endoplasmic reticulum and provokes its unique enlargement
    • Biemans, R., Thines, D., Rutgers, T., DeWilde, M., Cabezon, T. 1991. The large surface protein of hepatitis B virus is retained in the yeast endoplasmic reticulum and provokes its unique enlargement. DNA Cell. Biol. 10: 191-200.
    • (1991) DNA Cell. Biol. , vol.10 , pp. 191-200
    • Biemans, R.1    Thines, D.2    Rutgers, T.3    DeWilde, M.4    Cabezon, T.5
  • 5
    • 15444377148 scopus 로고
    • Yeast systems for the commercial production of heterologous proteins
    • Buckholz, R. G., Gleeson, M. A. G. 1991. Yeast systems for the commercial production of heterologous proteins. Bio/Technology 9: 1067-1072.
    • (1991) Bio/Technology , vol.9 , pp. 1067-1072
    • Buckholz, R.G.1    Gleeson, M.A.G.2
  • 6
    • 0023442396 scopus 로고
    • Regulation of sugar utilization in Saccharomyces species
    • Carlson, M. 1987. Regulation of sugar utilization in Saccharomyces species. J. Bacteriol. 169: 4873-4877.
    • (1987) J. Bacteriol. , vol.169 , pp. 4873-4877
    • Carlson, M.1
  • 7
    • 0023314418 scopus 로고
    • Secretion of heterologous proteins from Saccharomyces cerevisiae
    • Das, R. C., Shultz, J. L. 1987. Secretion of heterologous proteins from Saccharomyces cerevisiae. Biotechnol. Prog. 3(1): 43-48.
    • (1987) Biotechnol. Prog. , vol.3 , Issue.1 , pp. 43-48
    • Das, R.C.1    Shultz, J.L.2
  • 8
    • 0024400444 scopus 로고
    • Secretion of glycosylated human erythropoietin from yeast directed by the α-factor leader region
    • Elliott, S., Giffin, J., Suggs, S, Lau, E. P., Banks, A. R. 1989. Secretion of glycosylated human erythropoietin from yeast directed by the α-factor leader region. Gene 79: 167-180.
    • (1989) Gene , vol.79 , pp. 167-180
    • Elliott, S.1    Giffin, J.2    Suggs, S.3    Lau, E.P.4    Banks, A.R.5
  • 9
    • 2642638689 scopus 로고
    • Enzyme expression during growth and cell division in Saccharomyces cerevisiae: A study of galactose and phosphorus metabolism
    • Academic Press, New York
    • Halvorson, H. O., Botstian, K. A., Yarger, J. G., Hopper, J. E. 1984. Enzyme expression during growth and cell division in Saccharomyces cerevisiae: A study of galactose and phosphorus metabolism, pp. 49-86. In: Recombinant DNA and cell proliferation. Academic Press, New York.
    • (1984) Recombinant DNA and Cell Proliferation , pp. 49-86
    • Halvorson, H.O.1    Botstian, K.A.2    Yarger, J.G.3    Hopper, J.E.4
  • 10
    • 0028836667 scopus 로고
    • In vitro bioassay with enhanced sensitivity for human granulocyte colony-stimulating factor
    • Hammerling, U., Kroon, R., Sjodin, L. 1995. In vitro bioassay with enhanced sensitivity for human granulocyte colony-stimulating factor. J. Pharm. Biomed. Anal. 13 (1): 9-20.
    • (1995) J. Pharm. Biomed. Anal. , vol.13 , Issue.1 , pp. 9-20
    • Hammerling, U.1    Kroon, R.2    Sjodin, L.3
  • 13
    • 0021713896 scopus 로고
    • Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-α-factor
    • Julius, D., Brake, A., Blair, L., Kunisawa, R., Thorner, J. 1984. Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-α-factor. Cell 37: 1075-1089.
    • (1984) Cell , vol.37 , pp. 1075-1089
    • Julius, D.1    Brake, A.2    Blair, L.3    Kunisawa, R.4    Thorner, J.5
  • 14
    • 0023287617 scopus 로고
    • The production of mammalian proteins in Saccharomyces cerevisiae
    • Kingsman, S. M., Kingsman, A. J., Mellor, J. 1987. The production of mammalian proteins in Saccharomyces cerevisiae. Trends Biotechnol. 5: 53-57.
    • (1987) Trends Biotechnol. , vol.5 , pp. 53-57
    • Kingsman, S.M.1    Kingsman, A.J.2    Mellor, J.3
  • 15
    • 0022592345 scopus 로고
    • The stability of the yeast plasmid pJDB248 depends on growth rate of the culture
    • Kleinman, M. J., Gingold, E. B., Stanbury, P. F. 1986. The stability of the yeast plasmid pJDB248 depends on growth rate of the culture. Biotechnol. Lett. 8 (4): 225-230.
    • (1986) Biotechnol. Lett. , vol.8 , Issue.4 , pp. 225-230
    • Kleinman, M.J.1    Gingold, E.B.2    Stanbury, P.F.3
  • 16
    • 0025266783 scopus 로고
    • Structural characterization of natural and recombinant human granulocyte colony-stimulating factors
    • Kubota, N., Orita, T., Hattori, K., Oh-eda, M., Ochi, N., Yamazaki, T. 1990. Structural characterization of natural and recombinant human granulocyte colony-stimulating factors. J. Biochem. 107: 486-492.
    • (1990) J. Biochem. , vol.107 , pp. 486-492
    • Kubota, N.1    Orita, T.2    Hattori, K.3    Oh-eda, M.4    Ochi, N.5    Yamazaki, T.6
  • 17
    • 0020595853 scopus 로고
    • Hepatoma secretory proteins migrate from the rough endoplasmic reticulum to Golgi at characteristic rates
    • Lodish, H. F., Kong, N., Snider, M., Strous, G. J. A. M. 1983. Hepatoma secretory proteins migrate from the rough endoplasmic reticulum to Golgi at characteristic rates. Nature 304: 80-83.
    • (1983) Nature , vol.304 , pp. 80-83
    • Lodish, H.F.1    Kong, N.2    Snider, M.3    Strous, G.J.A.M.4
  • 18
    • 0021989397 scopus 로고
    • Factors affecting heterologous gene expression in Saccharomyces cerevisiae
    • Mellor, J., Dobson, M. J., Roberts, N. A., Kingsman, A. J., Kingsman, S. M. 1985. Factors affecting heterologous gene expression in Saccharomyces cerevisiae. Gene 33: 215-226.
    • (1985) Gene , vol.33 , pp. 215-226
    • Mellor, J.1    Dobson, M.J.2    Roberts, N.A.3    Kingsman, A.J.4    Kingsman, S.M.5
  • 20
    • 0025284968 scopus 로고
    • O-linked sugar chain of human granulocyte colony-stimulating factor protects it against polymerization and denaturation allowing it to retain its biological activity
    • Oh-eda, M., Hasegawa, M., Hattori, K., Kuboniwa, H., Kojima, T., Orita. T., Tomonou, K., Yamazaki, T., Ochi, N. 1990. O-linked sugar chain of human granulocyte colony-stimulating factor protects it against polymerization and denaturation allowing it to retain its biological activity. J. Biol. Chem. 265: 11432-11435.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11432-11435
    • Oh-eda, M.1    Hasegawa, M.2    Hattori, K.3    Kuboniwa, H.4    Kojima, T.5    Orita, T.6    Tomonou, K.7    Yamazaki, T.8    Ochi, N.9
  • 21
    • 0000688404 scopus 로고
    • Regulatory circuits for gene expression: The metabolism of galactose and phosphate
    • J. N. Strathern. E. W. Jones, and J. R. Broach, (eds.), Cold Spring Harbor Laboratory Press, Plainview, NY
    • Oshima, Y. 1982. Regulatory circuits for gene expression: The metabolism of galactose and phosphate, pp. 159-180. In: J. N. Strathern. E. W. Jones, and J. R. Broach, (eds.), The molecular biology of the yeast Saccharomyces: Metabolism and gene expression. Cold Spring Harbor Laboratory Press, Plainview, NY.
    • (1982) The Molecular Biology of the Yeast Saccharomyces: Metabolism and Gene Expression , pp. 159-180
    • Oshima, Y.1
  • 22
    • 0023644445 scopus 로고
    • Effect of growth rate and expression level on plasmid stability in Saccharomyces cerevisiae
    • Parker, C., DiBiasio, D. 1987. Effect of growth rate and expression level on plasmid stability in Saccharomyces cerevisiae. Biotechnol. Bioeng. 29 (2): 215-221.
    • (1987) Biotechnol. Bioeng. , vol.29 , Issue.2 , pp. 215-221
    • Parker, C.1    DiBiasio, D.2
  • 23
    • 0029257263 scopus 로고
    • Constitutive overexpression of secreted heterologous proteins decreases extractable BiP and protein disulfide isomerase levels in Saccharomyces cerevisiae
    • Robinson, A. S., Wittrup, K. D. 1995. Constitutive overexpression of secreted heterologous proteins decreases extractable BiP and protein disulfide isomerase levels in Saccharomyces cerevisiae. Biotechnol. Prog. 11: 171-177.
    • (1995) Biotechnol. Prog. , vol.11 , pp. 171-177
    • Robinson, A.S.1    Wittrup, K.D.2
  • 25
    • 2642710836 scopus 로고
    • Relationship between synthesis rate and secretion of GCSF expressed in yeast using a tunable delta integration vector
    • Anaheim. CA, April 2-6. American Chemical Society, Washington, DC
    • Shaw, M. R., Wittrup, K. D. 1995. Relationship between synthesis rate and secretion of GCSF expressed in yeast using a tunable delta integration vector. In: Abstracts of Papers of the 209th National Meeting of the American Chemical Society. Anaheim. CA, April 2-6. American Chemical Society, Washington, DC.
    • (1995) Abstracts of Papers of the 209th National Meeting of the American Chemical Society
    • Shaw, M.R.1    Wittrup, K.D.2
  • 26
    • 0026232555 scopus 로고
    • Gene expression in yeast: Protein secretion
    • Shuster, J. R. 1991. Gene expression in yeast: Protein secretion. Curr. Opin. Biotechnol. 2: 685-690.
    • (1991) Curr. Opin. Biotechnol. , vol.2 , pp. 685-690
    • Shuster, J.R.1
  • 27
    • 11944261204 scopus 로고
    • The secretion of human serum albumin from the yeast Saccharomyces cerevisiae using five different leader sequences
    • Sleep, D., Belfield, G. P., Goodey, A. R. 1990. The secretion of human serum albumin from the yeast Saccharomyces cerevisiae using five different leader sequences. Bio/Technology 8: 42-46.
    • (1990) Bio/Technology , vol.8 , pp. 42-46
    • Sleep, D.1    Belfield, G.P.2    Goodey, A.R.3
  • 28
    • 0021878793 scopus 로고
    • Heterologous protein secretion from yeast
    • Smith, R. A., Duncan, M. J., Moir, D. T. 1985. Heterologous protein secretion from yeast. Science 229: 1219-1224.
    • (1985) Science , vol.229 , pp. 1219-1224
    • Smith, R.A.1    Duncan, M.J.2    Moir, D.T.3
  • 29
    • 0021251554 scopus 로고
    • Double-stranded ribonucleic acid killer systems in yeasts
    • Tipper, D. J., Bostian, K. A. 1984. Double-stranded ribonucleic acid killer systems in yeasts. Microbiol. Rev. 48: 125-156.
    • (1984) Microbiol. Rev. , vol.48 , pp. 125-156
    • Tipper, D.J.1    Bostian, K.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.