메뉴 건너뛰기




Volumn 18, Issue 5, 1998, Pages 287-295

The glycosylation heterogeneity of recombinant human IFN-γ

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; GLYCOPROTEIN; MONOCLONAL ANTIBODY; RECOMBINANT GAMMA INTERFERON;

EID: 0031979830     PISSN: 10799907     EISSN: None     Source Type: Journal    
DOI: 10.1089/jir.1998.18.287     Document Type: Review
Times cited : (33)

References (53)
  • 1
    • 0000520727 scopus 로고
    • Virus interference 1. The interferon
    • ISAACS, A., and LINDENMANN, J. (1957). Virus interference 1. The interferon. Proc. Soc. Lond. [B] 147, 258-267.
    • (1957) Proc. Soc. Lond. [B] , vol.147 , pp. 258-267
    • Isaacs, A.1    Lindenmann, J.2
  • 2
    • 33845772515 scopus 로고
    • Interferon-like virus inhibitor induced in human leukocytes by phytohemagglutinin
    • WHEELOCK, E.F. (1965). Interferon-like virus inhibitor induced in human leukocytes by phytohemagglutinin. Science 149, 310-311.
    • (1965) Science , vol.149 , pp. 310-311
    • Wheelock, E.F.1
  • 3
    • 0027411525 scopus 로고
    • The molecular cell biology of interferon-γ and its receptor
    • FARRAR, M.A., and SCHREIBER, R.D. (1993). The molecular cell biology of interferon-γ and its receptor. Annu. Rev. Immunol. 11, 571-611.
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 571-611
    • Farrar, M.A.1    Schreiber, R.D.2
  • 5
    • 0022353320 scopus 로고
    • Structure and effects of interferon-gamma
    • ADOLF, G.R. (1985). Structure and effects of interferon-gamma. Oncology 42, 33-40.
    • (1985) Oncology , vol.42 , pp. 33-40
    • Adolf, G.R.1
  • 7
    • 0020489793 scopus 로고
    • Molecular cloning of human immune interferon cDNA and its expression in eukaryotic cells
    • DEVOS, R., CHEROUTRE, H., TAYA, Y., DEGRAVE, W., VAN HEUVERSWYN, H., and FIERS, W. (1982). Molecular cloning of human immune interferon cDNA and its expression in eukaryotic cells. Nucleic Acids Res. 10, 2487-2501.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 2487-2501
    • Devos, R.1    Cheroutre, H.2    Taya, Y.3    Degrave, W.4    Van Heuverswyn, H.5    Fiers, W.6
  • 8
    • 0006468313 scopus 로고
    • Cloning and expression of murine immune interferon cDNA
    • GRAY, P.W., and GOEDDEL, D.V. (1983). Cloning and expression of murine immune interferon cDNA. Proc. Natl. Acad. Sci. USA 80, 5842-5863.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 5842-5863
    • Gray, P.W.1    Goeddel, D.V.2
  • 10
    • 0021191796 scopus 로고
    • Natural human interferon-gamma. Complete amino acid sequence and determination of sites of glycosylation
    • RINDERKNECKT, E., O'CONNOR, B.H., and RODRIGUEZ, H. (1984). Natural human interferon-gamma. Complete amino acid sequence and determination of sites of glycosylation. J. Biol. Chem. 259, 6790-6797.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6790-6797
    • Rinderkneckt, E.1    O'Connor, B.H.2    Rodriguez, H.3
  • 12
    • 0020589423 scopus 로고
    • Molecular weight of the functional unit of human leukocyte, fibroblast and immune interferons
    • PESTKA, S., KELDER, B., FAMILLETTI, P.C., MOSCHERA, J.A., CROWL, R., and KEMPNER, E.S. (1983). Molecular weight of the functional unit of human leukocyte, fibroblast and immune interferons. J. Biol. Chem. 258, 9706-9709.
    • (1983) J. Biol. Chem. , vol.258 , pp. 9706-9709
    • Pestka, S.1    Kelder, B.2    Familletti, P.C.3    Moschera, J.A.4    Crowl, R.5    Kempner, E.S.6
  • 13
    • 0028342833 scopus 로고
    • Radiation inactivation of human gamma-interferon: Cellular activation requires two dimers
    • LANGER, J.A., RASHIDBAIGI, A., GAROTTA, G., and KEMPNER, E. (1994). Radiation inactivation of human gamma-interferon: cellular activation requires two dimers. Proc. Natl. Acad. Sci. USA 91, 5818-5822.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5818-5822
    • Langer, J.A.1    Rashidbaigi, A.2    Garotta, G.3    Kempner, E.4
  • 16
    • 0026701647 scopus 로고
    • Glycoprotein glycans - Roles and controls
    • GEISOW, M.J. (1992). Glycoprotein glycans - roles and controls. Trends Biotechnol. 10, 333-335.
    • (1992) Trends Biotechnol. , vol.10 , pp. 333-335
    • Geisow, M.J.1
  • 17
    • 0026848764 scopus 로고
    • Glycoprotein pharmaceuticals - Scientific and regultory considerations and the United States Orphan Drug Act
    • LIU, D.T.Y. (1992). Glycoprotein pharmaceuticals - scientific and regultory considerations and the United States Orphan Drug Act. Trends Biotechnol. 10, 114-120.
    • (1992) Trends Biotechnol. , vol.10 , pp. 114-120
    • Liu, D.T.Y.1
  • 18
    • 0029837484 scopus 로고    scopus 로고
    • Getting the glycosylation right - Implications for the biotechnology industry
    • JENKINS, N., PAREKH, R.B., and JAMES, D.C. (1996). Getting the glycosylation right - implications for the biotechnology industry. Nature Biotechnol. 14, 975-981.
    • (1996) Nature Biotechnol. , vol.14 , pp. 975-981
    • Jenkins, N.1    Parekh, R.B.2    James, D.C.3
  • 19
    • 0030292384 scopus 로고    scopus 로고
    • FDA, reform, and the well-characterized biologic
    • HENRY, C. (1996). FDA, reform, and the well-characterized biologic. Anal. Chem. News Features 674A-677A.
    • (1996) Anal. Chem. News Features
    • Henry, C.1
  • 20
    • 0028224656 scopus 로고
    • Glycosylation of recombinant proteins: Problems and prospects
    • JENKINS, N., and CURLING, E.M. (1994). Glycosylation of recombinant proteins: problems and prospects. Enz. Microb. Technol. 16, 354-364.
    • (1994) Enz. Microb. Technol. , vol.16 , pp. 354-364
    • Jenkins, N.1    Curling, E.M.2
  • 21
    • 0029563888 scopus 로고
    • Glycosylation and biological activity of Campath-1H expressed in different cell lines and grown under different culture conditions
    • LIFELY, M.R., HALE, C., BOYCE, S. KEEN, M.J., and PHILLIPS, J. (1995). Glycosylation and biological activity of Campath-1H expressed in different cell lines and grown under different culture conditions. Glycobiology 5, 813-822.
    • (1995) Glycobiology , vol.5 , pp. 813-822
    • Lifely, M.R.1    Hale, C.2    Boyce, S.3    Keen, M.J.4    Phillips, J.5
  • 22
    • 0027082659 scopus 로고
    • Differential inactivation of interferons by a protease from human granulocytes
    • CANTELL, K., HIRVONEN, S., SARENEVA, T., PIRHHONEN, J., and JULKUNEN, I. (1992). Differential inactivation of interferons by a protease from human granulocytes. J. Interferon Res. 12, 175-182.
    • (1992) J. Interferon Res. , vol.12 , pp. 175-182
    • Cantell, K.1    Hirvonen, S.2    Sareneva, T.3    Pirhhonen, J.4    Julkunen, I.5
  • 24
    • 0022555788 scopus 로고
    • A sandwich radioimmunoassay for human IFN-γ
    • KELDER, B., RASHIDBAIGI, A., and PESTKA, S. (1986). A sandwich radioimmunoassay for human IFN-γ. Methods Enzymol. 119, 582-587.
    • (1986) Methods Enzymol. , vol.119 , pp. 582-587
    • Kelder, B.1    Rashidbaigi, A.2    Pestka, S.3
  • 25
    • 0023370707 scopus 로고
    • A simple, rapid and large capacity ELISA for biologically active native and recombinant human IFN-γ
    • GALLATI, H., PRACHT, I., SCHMIDT, J., HARING, P., and GAROTTA, G. (1987). A simple, rapid and large capacity ELISA for biologically active native and recombinant human IFN-γ. J. Biol. Regul. Homeostat. Agents 1, 109-118.
    • (1987) J. Biol. Regul. Homeostat. Agents , vol.1 , pp. 109-118
    • Gallati, H.1    Pracht, I.2    Schmidt, J.3    Haring, P.4    Garotta, G.5
  • 28
    • 0025649375 scopus 로고
    • Recombinant human interferon-γ. Differences in glycosylation and proteolytic processing lead to heterogeneity in batch culture
    • CURLING, E.M., HAYTER, B.M., BAINES, A.J., BULL, A.T., GULL, K., STRANGE, P.G., and JENKINS, N. (1990). Recombinant human interferon-γ. Differences in glycosylation and proteolytic processing lead to heterogeneity in batch culture. Biochem. J. 272, 333-337.
    • (1990) Biochem. J. , vol.272 , pp. 333-337
    • Curling, E.M.1    Hayter, B.M.2    Baines, A.J.3    Bull, A.T.4    Gull, K.5    Strange, P.G.6    Jenkins, N.7
  • 29
    • 0028173035 scopus 로고
    • High-resolution separation of recombinant human interferon-γ glycoforms by micellar electrokinetic capillary chromatography
    • JAMES, D.C., FREEDMAN, R.B., HOARE, M., and JENKINS, N. (1994). High-resolution separation of recombinant human interferon-γ glycoforms by micellar electrokinetic capillary chromatography. Anal. Biochem. 222, 315-322.
    • (1994) Anal. Biochem. , vol.222 , pp. 315-322
    • James, D.C.1    Freedman, R.B.2    Hoare, M.3    Jenkins, N.4
  • 30
    • 0025863629 scopus 로고
    • High performance capillary electrophoresis
    • FRENZ, J., and HANCOCK, W.S. (1991). High performance capillary electrophoresis. Trends Biotechnol. 9, 243-250.
    • (1991) Trends Biotechnol. , vol.9 , pp. 243-250
    • Frenz, J.1    Hancock, W.S.2
  • 31
    • 0027189935 scopus 로고
    • High performance capillary electrophoresis of glycoconjugates
    • NOVOTNY, M.V., and SUDOR, J. (1993). High performance capillary electrophoresis of glycoconjugates. Electrophoresis 14, 372-389.
    • (1993) Electrophoresis , vol.14 , pp. 372-389
    • Novotny, M.V.1    Sudor, J.2
  • 32
    • 0026578211 scopus 로고
    • Separation and analysis of the glycoform populations of ribonuclease b using capillary electrophoresis
    • RUDD, P.M., SCRAGG, I.G., COGHILI, E., and DWEK, R.A. (1992). Separation and analysis of the glycoform populations of ribonuclease b using capillary electrophoresis. Glycoconjugate J. 9, 86-91.
    • (1992) Glycoconjugate J. , vol.9 , pp. 86-91
    • Rudd, P.M.1    Scragg, I.G.2    Coghili, E.3    Dwek, R.A.4
  • 33
    • 0029996036 scopus 로고    scopus 로고
    • Recent advances in capillary electrophoresis of carbohydrates
    • EL-RASSI, Z., and MECHREF, Y. (1996). Recent advances in capillary electrophoresis of carbohydrates. Electrophoresis 17, 275-301.
    • (1996) Electrophoresis , vol.17 , pp. 275-301
    • El-Rassi, Z.1    Mechref, Y.2
  • 37
    • 0026574265 scopus 로고
    • Analysis of the five glycosylation sites of human α1-acid glycoprotein
    • TREUHEIT, M.J., COSTELLO, C.E., and HALSALL, H.B. (1992). Analysis of the five glycosylation sites of human α1-acid glycoprotein. Biochem. J. 283, 105-112.
    • (1992) Biochem. J. , vol.283 , pp. 105-112
    • Treuheit, M.J.1    Costello, C.E.2    Halsall, H.B.3
  • 39
    • 0028349781 scopus 로고
    • Site specific characterization of glycoprotein carbohydrates by exoglycosidase digestion and laser desorption mass spectroscopy
    • SUTTON, C.W., O'NEILL, J., and COTTRELL, J.S. (1994). Site specific characterization of glycoprotein carbohydrates by exoglycosidase digestion and laser desorption mass spectroscopy. Anal. Biochem. 218, 34-46.
    • (1994) Anal. Biochem. , vol.218 , pp. 34-46
    • Sutton, C.W.1    O'Neill, J.2    Cottrell, J.S.3
  • 43
    • 0030048495 scopus 로고    scopus 로고
    • Mass spectrometric characterization of glycosylated interferon-γ variants by gel electrophoresis
    • MORTZ, E., SARENEVA, T., HAEBEL, S., JULKUNEN, I., and ROEPSTORFF, P. (1996). Mass spectrometric characterization of glycosylated interferon-γ variants by gel electrophoresis. Electrophoresis 17, 925-931.
    • (1996) Electrophoresis , vol.17 , pp. 925-931
    • Mortz, E.1    Sareneva, T.2    Haebel, S.3    Julkunen, I.4    Roepstorff, P.5
  • 44
    • 34548374880 scopus 로고    scopus 로고
    • Microheterogeneity of N-linked carbohydrates in natural interferon-γ characterized by matrix assisted laser desorption ionization mass spectrometry
    • In press
    • MORTZ, E., SARENEVA, T., JULKUNEN, I., and ROEPSTORFF, P. (1997). Microheterogeneity of N-linked carbohydrates in natural interferon-γ characterized by matrix assisted laser desorption ionization mass spectrometry. J. Mass Spectrom. In press.
    • (1997) J. Mass Spectrom.
    • Mortz, E.1    Sareneva, T.2    Julkunen, I.3    Roepstorff, P.4
  • 45
    • 0030014292 scopus 로고    scopus 로고
    • Rapid monitoring of site-specific glycosylation microheterogeneity of recombinant human interferon-γ
    • HARMON, B.J., XUEJUN, G.U., and WANG, D.I.C. (1996). Rapid monitoring of site-specific glycosylation microheterogeneity of recombinant human interferon-γ. Anal. Chem. 68, 1465-1473.
    • (1996) Anal. Chem. , vol.68 , pp. 1465-1473
    • Harmon, B.J.1    Xuejun, G.U.2    Wang, D.I.C.3
  • 46
    • 0030893157 scopus 로고    scopus 로고
    • Monitoring proteolysis of recombinant human interferon-γ during batch culture of Chinese hamster ovary cells
    • GOLDMAN, M.H., JAMES, D.C., ISON, A.P., and BULL, A.T. (1997). Monitoring proteolysis of recombinant human interferon-γ during batch culture of Chinese hamster ovary cells. Cytotechnology 23, 103-111.
    • (1997) Cytotechnology , vol.23 , pp. 103-111
    • Goldman, M.H.1    James, D.C.2    Ison, A.P.3    Bull, A.T.4
  • 47
    • 0024552682 scopus 로고
    • Study of the primary structure of recombinant tissue plasminogen activator by reversed-phase high performance liquid ChromatographiC tryptic mapping
    • CHLOUPEK, R.C., HARRIS, R.J., LEONARD, C.K., KECK, R.G., KEYT, B.A., SPELLMAN, M.W., JONES, J.S., and HANCOCK, W.S. (1989). Study of the primary structure of recombinant tissue plasminogen activator by reversed-phase high performance liquid ChromatographiC tryptic mapping. J. Chromatogr. 463, 375-396.
    • (1989) J. Chromatogr. , vol.463 , pp. 375-396
    • Chloupek, R.C.1    Harris, R.J.2    Leonard, C.K.3    Keck, R.G.4    Keyt, B.A.5    Spellman, M.W.6    Jones, J.S.7    Hancock, W.S.8
  • 49
    • 0023885012 scopus 로고
    • Role of the carboxy-terminal sequence on the biological activity of human immune interferon (IFN-γ)
    • DOBELI, H., GENTZ, R., JUCKER, W., GAROTTA, G., HARTMANN, D.W., and HOCHULI, E. (1988). Role of the carboxy-terminal sequence on the biological activity of human immune interferon (IFN-γ). J. Biotechnol. 7, 199-216.
    • (1988) J. Biotechnol. , vol.7 , pp. 199-216
    • Dobeli, H.1    Gentz, R.2    Jucker, W.3    Garotta, G.4    Hartmann, D.W.5    Hochuli, E.6
  • 50
    • 0026093103 scopus 로고
    • The carboxyl-terminal of human interferon-gamma is important for biological activity - Mutagenic and NMR analysis
    • LUNDELL, D., LUNN, C., DELGANO, D., FOSSETTA, J., GREENBERG, R., REIM, R., GRACE, M., and NARULA, S. (1991). The carboxyl-terminal of human interferon-gamma is important for biological activity - mutagenic and NMR analysis. Protein Eng. 5, 335-341.
    • (1991) Protein Eng. , vol.5 , pp. 335-341
    • Lundell, D.1    Lunn, C.2    Delgano, D.3    Fossetta, J.4    Greenberg, R.5    Reim, R.6    Grace, M.7    Narula, S.8
  • 51
    • 0030070842 scopus 로고    scopus 로고
    • Isolation and characterization of an insect-cell line able to perform complex N-linked glycosylation on recombinant proteins
    • OGONAH, O.W., FREEDMAN, R.B., JENKINS, N., PATEL, K., and ROONEY, B.C. (1996). Isolation and characterization of an insect-cell line able to perform complex N-linked glycosylation on recombinant proteins. Bio/Technology 14, 197-202.
    • (1996) Bio/Technology , vol.14 , pp. 197-202
    • Ogonah, O.W.1    Freedman, R.B.2    Jenkins, N.3    Patel, K.4    Rooney, B.C.5
  • 52
    • 0026342559 scopus 로고
    • Clearing up glycoprotein hormones
    • DRICKAMER, K. (1991). Clearing up glycoprotein hormones. Cell 67, 1029-1032.
    • (1991) Cell , vol.67 , pp. 1029-1032
    • Drickamer, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.