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Volumn 308, Issue 2, 2002, Pages 232-238

A technique for isolation of rubella virus-like particles by sucrose gradient ultracentrifugation using Coomassie brilliant blue G crystals

Author keywords

Coomassie brilliant blue G; Crystals; Rubella virus like particles; Sucrose gradient ultracentrifugation

Indexed keywords

CELL CULTURE; CENTRIFUGATION; MICROFILTRATION; PELLETIZING; PROTEINS; SUGAR (SUCROSE); VIRUSES;

EID: 0037108829     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0003-2697(02)00217-8     Document Type: Article
Times cited : (7)

References (24)
  • 1
    • 0025039837 scopus 로고
    • Processing and intracellular transport of rubella virus structural proteins in COS cells
    • T.C. Hobman, M.L. Lundstrom, S. Gillam, Processing and intracellular transport of rubella virus structural proteins in COS cells, Virology 178 (1990) 122-133.
    • (1990) Virology , vol.178 , pp. 122-133
    • Hobman, T.C.1    Lundstrom, M.L.2    Gillam, S.3
  • 2
    • 0028065160 scopus 로고
    • Assembly of rubella virus structural proteins into virus-like particles in transfected cells
    • T.C. Hobman, M.L. Lundstrom, C.A. Mauracher, L. Woodward, S. Gillam, M.G. Farquhar, Assembly of rubella virus structural proteins into virus-like particles in transfected cells, Virology 202 (1994) 574-585.
    • (1994) Virology , vol.202 , pp. 574-585
    • Hobman, T.C.1    Lundstrom, M.L.2    Mauracher, C.A.3    Woodward, L.4    Gillam, S.5    Farquhar, M.G.6
  • 3
    • 0028226159 scopus 로고
    • Expression and characterisation of virus-like particles containing rubella virus structural proteins
    • Z. Qui, D. Ou, H. Wu, T.C. Hobman, S. Gillam, Expression and characterisation of virus-like particles containing rubella virus structural proteins, J. Virol. 68 (1994) 4086-4091.
    • (1994) J. Virol. , vol.68 , pp. 4086-4091
    • Qui, Z.1    Ou, D.2    Wu, H.3    Hobman, T.C.4    Gillam, S.5
  • 4
    • 0020626190 scopus 로고
    • Immunochemical identification of rubella virus hemagglutinin
    • M.N. Waxham, J.S. Wolinsky, Immunochemical identification of rubella virus hemagglutinin, Virology 126 (1983) 194-203.
    • (1983) Virology , vol.126 , pp. 194-203
    • Waxham, M.N.1    Wolinsky, J.S.2
  • 5
    • 0000871532 scopus 로고    scopus 로고
    • Rubella
    • B.N. Fields, D.M. Knipe, P.M. Howley (Eds.), Lippincott-Raven Publisher, Philadelphia
    • J.S. Wolinsky, Rubella, in: B.N. Fields, D.M. Knipe, P.M. Howley (Eds.), Fields Virology, Lippincott-Raven Publisher, Philadelphia, 1996, pp. 899-929.
    • (1996) Fields Virology , pp. 899-929
    • Wolinsky, J.S.1
  • 6
    • 0000853902 scopus 로고
    • A model of the structural organization of rubella virions
    • M.N. Waxham, J.S. Wolinsky, A model of the structural organization of rubella virions, Rev. Infect. Dis. 7 (1) (1985) 133-139.
    • (1985) Rev. Infect. Dis. , vol.7 , Issue.1 , pp. 133-139
    • Waxham, M.N.1    Wolinsky, J.S.2
  • 7
    • 0031036010 scopus 로고    scopus 로고
    • Evaluation of a new enzyme immunoassay based on recombinant rubella virus-like particles for detection of immunoglobulin M antibodies to rubella virus
    • L. Grangeot-Keros, G. Enders, Evaluation of a new enzyme immunoassay based on recombinant rubella virus-like particles for detection of immunoglobulin M antibodies to rubella virus, J. Clin. Microbiol. 35 (1997) 398-401.
    • (1997) J. Clin. Microbiol. , vol.35 , pp. 398-401
    • Grangeot-Keros, L.1    Enders, G.2
  • 8
    • 0029964288 scopus 로고    scopus 로고
    • Evaluation of recombinant rubella-like particles in commercial immunoassay for the detection of anti-rubella IgG
    • B. Pustowoit, L. Grangeot-Keros, T.C. Hobman, J. Hofmann, Evaluation of recombinant rubella-like particles in commercial immunoassay for the detection of anti-rubella IgG, Clin. Diagn. Virol. 5 (1996) 13-20.
    • (1996) Clin. Diagn. Virol. , vol.5 , pp. 13-20
    • Pustowoit, B.1    Grangeot-Keros, L.2    Hobman, T.C.3    Hofmann, J.4
  • 9
    • 0026511956 scopus 로고
    • Detection of rubella virus-specific immunoglobulin G (IgG), IgM, and IgA antibodies by immunoblot assays
    • T. Zhang, C.A. Mauracher, L.A. Mitchell, A.J. Tingle, Detection of rubella virus-specific immunoglobulin G (IgG), IgM, and IgA antibodies by immunoblot assays, J. Clin. Microbiol. 30 (1992) 824-830.
    • (1992) J. Clin. Microbiol. , vol.30 , pp. 824-830
    • Zhang, T.1    Mauracher, C.A.2    Mitchell, L.A.3    Tingle, A.J.4
  • 10
    • 0034931104 scopus 로고    scopus 로고
    • Quantitative and reproducable two-dimensional gel analysis using Phoretix 2D full
    • P. Mahon, P. Dupree, Quantitative and reproducable two-dimensional gel analysis using Phoretix 2D full, Electrophoresis 22 (2001) 2075-2085.
    • (2001) Electrophoresis , vol.22 , pp. 2075-2085
    • Mahon, P.1    Dupree, P.2
  • 11
    • 0028172974 scopus 로고
    • A staining procedure using Coomassie brilliant blue G-250 in phosphoric acid for detection of protein bands with high resolution in polyacrylamide gel and nitrocellulose membrane
    • P. Mitra, A.K. Pal, D. Basu, R.N. Hati, A staining procedure using Coomassie Brilliant Blue G-250 in phosphoric acid for detection of protein bands with high resolution in polyacrylamide gel and nitrocellulose membrane, Anal. Biochem. 223 (1994) 327-329.
    • (1994) Anal. Biochem. , vol.223 , pp. 327-329
    • Mitra, P.1    Pal, A.K.2    Basu, D.3    Hati, R.N.4
  • 12
    • 0028088232 scopus 로고
    • Quantitation of electrophoretically separated proteins in the submicrogram range by dye elution
    • U. Neumann, H. Khalaf, M. Rimpler, Quantitation of electrophoretically separated proteins in the submicrogram range by dye elution, Electrophoresis 15 (1994) 916-921.
    • (1994) Electrophoresis , vol.15 , pp. 916-921
    • Neumann, U.1    Khalaf, H.2    Rimpler, M.3
  • 13
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 14
    • 0027304549 scopus 로고
    • A comparison of the binding of Coomassie brilliant blue to proteins at low and neutral pH
    • H.J. Chial, A.G. Splittgerber, A comparison of the binding of Coomassie brilliant blue to proteins at low and neutral pH, Anal. Biochem. 213 (1993) 362-369.
    • (1993) Anal. Biochem. , vol.213 , pp. 362-369
    • Chial, H.J.1    Splittgerber, A.G.2
  • 15
    • 0026676350 scopus 로고
    • Recovery of protein by Coomassie brilliant blue precipitation prior to electrophoresis
    • T. Marshall, K.M. Williams, Recovery of protein by Coomassie brilliant blue precipitation prior to electrophoresis, Electrophoresis 13 (1992) 887-888.
    • (1992) Electrophoresis , vol.13 , pp. 887-888
    • Marshall, T.1    Williams, K.M.2
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • U.K. Lämmli, Cleavage of structural proteins during assembly of the head of bacteriophage T4, Nature 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Lämmli, U.K.1
  • 17
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • H. Blum, H. Beier, H.J. Gross, Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels, Electrophoresis 8 (1987) 93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 18
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • H.T. Towbin, T. Staehelin, J. Gordon, Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications, Proc. Natl. Acad. Sci. USA 76 (1979) 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.T.1    Staehelin, T.2    Gordon, J.3
  • 19
    • 0021321955 scopus 로고
    • A rapid, sensitive method for detection of alkaline phosphatase-conjugated antibody on Western blots
    • M.S. Blake, H.K. Johnston, G.J. Russell-Jones, E.C. Gotschlich, A rapid, sensitive method for detection of alkaline phosphatase-conjugated antibody on Western blots, Anal. Biochem. 136 (1984) 175-179.
    • (1984) Anal. Biochem. , vol.136 , pp. 175-179
    • Blake, M.S.1    Johnston, H.K.2    Russell-Jones, G.J.3    Gotschlich, E.C.4
  • 21
    • 0031041563 scopus 로고    scopus 로고
    • Monitoring cholesterol crystallization from lithogenic model bile by time-lapse density gradient ultracentrifugation
    • F.M. Konikoff, H. Laufer, G. Messer, T. Gilat, Monitoring cholesterol crystallization from lithogenic model bile by time-lapse density gradient ultracentrifugation, J. Hepatol. 26 (1997) 703-710.
    • (1997) J. Hepatol. , vol.26 , pp. 703-710
    • Konikoff, F.M.1    Laufer, H.2    Messer, G.3    Gilat, T.4
  • 22
    • 0030801315 scopus 로고    scopus 로고
    • Calcium and anionic polypeptide fraction (APF) have opposing effects on cholesterol crystallization in model bile
    • F.M. Konikoff, P. Lechene de la Porte, H. Laufer, N. Domingo, H. Lafont, T. Gilat, Calcium and anionic polypeptide fraction (APF) have opposing effects on cholesterol crystallization in model bile, J. Hepatol. 27 (1997) 707-715.
    • (1997) J. Hepatol. , vol.27 , pp. 707-715
    • Konikoff, F.M.1    Lechene de la Porte, P.2    Laufer, H.3    Domingo, N.4    Lafont, H.5    Gilat, T.6
  • 23
    • 0023230138 scopus 로고
    • Single spin density gradient ultracentrifugation method for the detection and isolation of light and heavy low density lipoprotein subfractions
    • D.W. Swinkels, H.L.M. Hak-Lemmers, P.N.M. Demacker, Single spin density gradient ultracentrifugation method for the detection and isolation of light and heavy low density lipoprotein subfractions, J. Lipid Res. 28 (1987) 1233-1239.
    • (1987) J. Lipid Res. , vol.28 , pp. 1233-1239
    • Swinkels, D.W.1    Hak-Lemmers, H.L.M.2    Demacker, P.N.M.3
  • 24
    • 0025218375 scopus 로고
    • Chromatography on immobilized reactive dyes
    • E. Stellwagen, Chromatography on immobilized reactive dyes, Methods Enzymol. 182 (1990) 343-357.
    • (1990) Methods Enzymol. , vol.182 , pp. 343-357
    • Stellwagen, E.1


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