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Volumn 45, Issue 6, 2010, Pages 612-617

MALDI linear TOF mass spectrometry of PEGylated (glyco)proteins

Author keywords

High mass ion detection; MALDI; Mass spectrometry; PEGylation; Recombinant proteins

Indexed keywords

COAGULATION FACTOR; DETECTOR SYSTEMS; GLYCOSYLATED; HIGH MOLECULAR MASS; HIGH MOLECULAR WEIGHT; HUMAN SERUM ALBUMINS; ION DETECTION; LASER DESORPTION/IONIZATION TIME OF FLIGHTS; LIFE-TIMES; MALDI TOF MS; MALDI-MASS SPECTROMETRY; PEGYLATION; PHARMACEUTICAL SCIENCE; PROTEIN PEGYLATION; RECOMBINANT PROTEIN; SECONDARY ELECTRON MULTIPLIERS; SEM; TOF MASS SPECTROMETRY; VON WILLEBRAND FACTOR;

EID: 77953156970     PISSN: 10765174     EISSN: 10969888     Source Type: Journal    
DOI: 10.1002/jms.1746     Document Type: Article
Times cited : (32)

References (40)
  • 1
    • 84875463071 scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers
    • F. Hillenkamp, M. Karas, R. C. Beavis, B. T. Chait. Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers. Anal. Chem. 1991, 63, 1193A.
    • (1991) Anal. Chem. , vol.63
    • Hillenkamp, F.1    Karas, M.2    Beavis, R.C.3    Chait, B.T.4
  • 2
    • 84984042980 scopus 로고
    • Protein and polymer analysis up tom/z 100 000 by laser ionization time-of-flight mass spectrometry
    • K. Tanaka, H. Waki, Y. Ido, S. Akita, Y. Yoshida, T. Yoshida. Protein and polymer analysis up tom/z 100 000 by laser ionization time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom. 1988, 2, 151.
    • (1988) Rapid Commun. Mass Spectrom. , vol.2 , pp. 151
    • Tanaka, K.1    Waki, H.2    Ido, Y.3    Akita, S.4    Yoshida, Y.5    Yoshida, T.6
  • 3
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • J. B. Fenn, M. Mann, C. K. Meng, S. F.Wong, C. M. Whitehouse. Electrospray ionization for mass spectrometry of large biomolecules. Science 1989, 246, 64.
    • (1989) Science , vol.246 , pp. 64
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 4
    • 0343775584 scopus 로고    scopus 로고
    • Ionization in matrix-assisted laser desorption/ionization: Singly charged molecular ions are the lucky survivors
    • M. Karas, M. Gluckmann, J. Schafer. Ionization in matrix-assisted laser desorption/ionization: singly charged molecular ions are the lucky survivors. J. Mass Spectrom. 2000, 35, 1.
    • (2000) J. Mass Spectrom. , vol.35 , pp. 1
    • Karas, M.1    Gluckmann, M.2    Schafer, J.3
  • 5
    • 67649726115 scopus 로고    scopus 로고
    • Characterization of high molecular weight multimeric states of human haptoglobin and hemoglobin-based oxygen carriers by high-mass MALDI MS
    • T. Pimenova, C. P. Pereira, D. J. Schaer, R. Zenobi. Characterization of high molecular weight multimeric states of human haptoglobin and hemoglobin-based oxygen carriers by high-mass MALDI MS. J. Sep. Sci. 2009, 32, 1224.
    • (2009) J. Sep. Sci. , vol.32 , pp. 1224
    • Pimenova, T.1    Pereira, C.P.2    Schaer, D.J.3    Zenobi, R.4
  • 6
    • 39749134756 scopus 로고    scopus 로고
    • Characterization of antibody-antigen interactions: Comparison between surface plasmon resonancemeasurements and high-mass matrix-assisted laser desorption/ionization mass spectrometry
    • C. Bich, M. Scott, A. Panagiotidis, R. J. Wenzel, A. Nazabal, R. Zenobi. Characterization of antibody-antigen interactions: comparison between surface plasmon resonancemeasurements and high-mass matrix-assisted laser desorption/ionization mass spectrometry. Anal. Biochem. 2008, 375, 35.
    • (2008) Anal. Biochem. , vol.375 , pp. 35
    • Bich, C.1    Scott, M.2    Panagiotidis, A.3    Wenzel, R.J.4    Nazabal, A.5    Zenobi, R.6
  • 7
    • 11844260047 scopus 로고    scopus 로고
    • Instrumental parameters in the MALDI-TOF mass spectrometric analysis of quaternary protein structures
    • M. Zehl, G. Allmaier. Instrumental parameters in the MALDI-TOF mass spectrometric analysis of quaternary protein structures. Anal. Chem. 2005, 77, 103.
    • (2005) Anal. Chem. , vol.77 , pp. 103
    • Zehl, M.1    Allmaier, G.2
  • 8
    • 33845587250 scopus 로고    scopus 로고
    • Molecular weight determination of ultrahigh mass compounds on a standard matrix-assisted laser desorption/ionization time-of-flight mass spectrometer: PAMAM dendrimer generation 10 and immunoglobulin M
    • R. Mueller, G. Allmaier. Molecular weight determination of ultrahigh mass compounds on a standard matrix-assisted laser desorption/ionization time-of-flight mass spectrometer: PAMAM dendrimer generation 10 and immunoglobulin M. Rapid Commun. Mass Spectrom. 2006, 20, 3803.
    • (2006) Rapid Commun. Mass Spectrom. , vol.20 , pp. 3803
    • Mueller, R.1    Allmaier, G.2
  • 9
    • 7544223646 scopus 로고    scopus 로고
    • Optical detection methods for mass spectrometry of macroions
    • W. P. Peng, Y. Cai, H. C. Chang. Optical detection methods for mass spectrometry of macroions. Mass Spectrom. Rev. 2004, 23, 443.
    • (2004) Mass Spectrom. Rev. , vol.23 , pp. 443
    • Peng, W.P.1    Cai, Y.2    Chang, H.C.3
  • 10
    • 0033126156 scopus 로고    scopus 로고
    • Energy-sensitive cryogenic detectors for high-mass biomoleculemass spectrometry
    • M. Frank, S. E. Labov, G. Westmacott, W. H. Benner. Energy-sensitive cryogenic detectors for high-mass biomoleculemass spectrometry. Mass Spectrom. Rev. 1999, 18, 155.
    • (1999) Mass Spectrom. Rev. , vol.18 , pp. 155
    • Frank, M.1    Labov, S.E.2    Westmacott, G.3    Benner, W.H.4
  • 11
    • 0018478296 scopus 로고
    • Microchannel plate detectors
    • J. Wiza. Microchannel plate detectors. Nucl. Instrum. Methods 1979, 162, 587.
    • (1979) Nucl. Instrum. Methods , vol.162 , pp. 587
    • Wiza, J.1
  • 12
    • 0030478314 scopus 로고    scopus 로고
    • High-efficiency detection of 66 000 Da proteinmolecules using a cryogenicdetector ina matrix-assisted laser desorption/ionization time-of-flightmass spectrometer
    • M. Frank, C. A. Mears, S. E. Labov, W. H. Benner, D. Horn, J. M. Jaklevic, A. T. Barfknecht. High-efficiency detection of 66 000 Da proteinmolecules using a cryogenicdetector ina matrix-assisted laser desorption/ionization time-of-flightmass spectrometer. Rapid Commun.Mass Spectrom. 1996, 10, 1946.
    • (1996) Rapid Commun.Mass Spectrom. , vol.10 , pp. 1946
    • Frank, M.1    Mears, C.A.2    Labov, S.E.3    Benner, W.H.4    Horn, D.5    Jaklevic, J.M.6    Barfknecht, A.T.7
  • 14
    • 27544477378 scopus 로고    scopus 로고
    • Analysis of megadalton ions using cryodetection MALDI time-of-flight mass spectrometry
    • R. J. Wenzel, U. Matter, L. Schultheis, R. Zenobi. Analysis of megadalton ions using cryodetection MALDI time-of-flight mass spectrometry. Anal. Chem. 2005, 77, 4329.
    • (2005) Anal. Chem. , vol.77 , pp. 4329
    • Wenzel, R.J.1    Matter, U.2    Schultheis, L.3    Zenobi, R.4
  • 16
    • 0001695717 scopus 로고    scopus 로고
    • Secondary ion and electron yield measurements for surfaces bombarded with large molecular ions
    • G. Westmacott, W. Ens, K. G. Standing. Secondary ion and electron yield measurements for surfaces bombarded with large molecular ions. Nucl. Instrum. Methods Phys. Res. Sect. B 1996, 108, 282.
    • (1996) Nucl. Instrum. Methods Phys. Res. Sect. B , vol.108 , pp. 282
    • Westmacott, G.1    Ens, W.2    Standing, K.G.3
  • 18
    • 0017701219 scopus 로고
    • Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol
    • A. Abuchowski, T. van Es, N. C. Palczuk, F. F. Davis. Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol. J. Biol. Chem. 1977, 252, 3578.
    • (1977) J. Biol. Chem. , vol.252 , pp. 3578
    • Abuchowski, A.1    Van Es, T.2    Palczuk, N.C.3    Davis, F.F.4
  • 19
    • 0029360545 scopus 로고
    • Chemistry of polyethylene glycol conjugates with biologically active molecules
    • S. Zalipsky. Chemistry of polyethylene glycol conjugates with biologically active molecules. Adv. Drug Delivery Rev. 1995, 16, 157.
    • (1995) Adv. Drug Delivery Rev. , vol.16 , pp. 157
    • Zalipsky, S.1
  • 20
    • 17844380498 scopus 로고    scopus 로고
    • Pegylation: A novel process for modifying pharmacokinetics
    • J. M. Harris, N. E. Martin, M. Modi. Pegylation: a novel process for modifying pharmacokinetics. Clin. Pharmacokinet. 2001, 40, 539.
    • (2001) Clin. Pharmacokinet. , vol.40 , pp. 539
    • Harris, J.M.1    Martin, N.E.2    Modi, M.3
  • 21
    • 0029888326 scopus 로고    scopus 로고
    • Improvement of pharmacokinetic, immunological and stability properties of asparaginase by conjugation to linear and branchedmonomethoxypoly (ethylene glycol)
    • F. M. Veronese,C. Monfardini, P. Calceti,O. Schiavon,M. D. Scrawen, D. Beer. Improvement of pharmacokinetic, immunological and stability properties of asparaginase by conjugation to linear and branchedmonomethoxypoly (ethylene glycol). J. Controlled Release 1996, 40, 199.
    • (1996) J. Controlled Release , vol.40 , pp. 199
    • Veronese, F.M.1    Monfardini, C.2    Calceti, P.3    Schiavon, O.4    Scrawen, M.D.5    Beer, D.6
  • 23
    • 0029783864 scopus 로고    scopus 로고
    • Characterization of poly(ethylene glycol)-modified superoxide dismutase: Comparison of capillary electrophoresis and matrix-assisted laser desorption/ionization mass spectrometry
    • J. Bullock, S. Chowdhury, D. Johnston. Characterization of poly(ethylene glycol)-modified superoxide dismutase: comparison of capillary electrophoresis and matrix-assisted laser desorption/ionization mass spectrometry. Anal. Chem. 1996, 68, 3258.
    • (1996) Anal. Chem. , vol.68 , pp. 3258
    • Bullock, J.1    Chowdhury, S.2    Johnston, D.3
  • 24
    • 33750617176 scopus 로고    scopus 로고
    • Precise and comparative pegylation analysis by microfluidics and mass spectrometry
    • T. Yu, J. A. Traina, E. Pungor, M. McCaman. Precise and comparative pegylation analysis by microfluidics and mass spectrometry. Anal. Biochem. 2006, 359, 54.
    • (2006) Anal. Biochem. , vol.359 , pp. 54
    • Yu, T.1    Traina, J.A.2    Pungor, E.3    McCaman, M.4
  • 30
    • 0037124508 scopus 로고    scopus 로고
    • Use of peginterferon alfa-2a (40 kDa) (Pegasys) for the treatmentofhepatitis C
    • R. K. Rajender, M.W. Modi, S. Pedder. Use of peginterferon alfa-2a (40 kDa) (Pegasys) for the treatmentofhepatitis C. Adv.Drug Delivery Rev. 2002, 54, 571.
    • (2002) Adv.Drug Delivery Rev. , vol.54 , pp. 571
    • Rajender, R.K.1    Modi, M.W.2    Pedder, S.3
  • 31
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • X. M. He, D. C. Carter. Atomic structure and chemistry of human serum albumin. Nature 1992, 358, 209.
    • (1992) Nature , vol.358 , pp. 209
    • He, X.M.1    Carter, D.C.2
  • 33
    • 0032402122 scopus 로고    scopus 로고
    • The life cycle of coagulation factor VIII in view of its structure and function
    • P. J. Lenting, J. A. van Mourik, K. Mertens. The life cycle of coagulation factor VIII in view of its structure and function. Blood 1998, 92, 3983.
    • (1998) Blood , vol.92 , pp. 3983
    • Lenting, P.J.1    Van Mourik, J.A.2    Mertens, K.3
  • 34
    • 0038362149 scopus 로고    scopus 로고
    • Coagulation factor VIII: Structure and stability
    • W. Wang, Y. J. Wang, D. N. Kelner. Coagulation factor VIII: structure and stability. Int. J. Pharm. 2003, 259, 1.
    • (2003) Int. J. Pharm. , vol.259 , pp. 1
    • Wang, W.1    Wang, Y.J.2    Kelner, D.N.3
  • 35
    • 33750825113 scopus 로고    scopus 로고
    • The protein structure and effect of factor VIII
    • H. Fang, L. Wang, H. Wang. The protein structure and effect of factor VIII. Thromb. Res. 2007, 119, 1.
    • (2007) Thromb. Res. , vol.119 , pp. 1
    • Fang, H.1    Wang, L.2    Wang, H.3
  • 36
    • 0026762462 scopus 로고
    • Biological regulation of factor VIII activity
    • R. J. Kaufman. Biological regulation of factor VIII activity. Annu. Rev. Med. 1992, 43, 325.
    • (1992) Annu. Rev. Med. , vol.43 , pp. 325
    • Kaufman, R.J.1
  • 37
    • 77953161455 scopus 로고    scopus 로고
    • In vitro and in vivo characterization of full-length rFVIII modifiedwith PEG via coupling to primary amino groups
    • P. L. Turecek, J. Siekmann, H. Gritsch, K. Varadi, R. U. Ahmad, E. M. Muchitsch, H. Ehrlich, H. P. Schwarz. In vitro and in vivo characterization of full-length rFVIII modifiedwith PEG via coupling to primary amino groups. Blood 2007, 110, 3147.
    • (2007) Blood , vol.110 , pp. 3147
    • Turecek, P.L.1    Siekmann, J.2    Gritsch, H.3    Varadi, K.4    Ahmad, R.U.5    Muchitsch, E.M.6    Ehrlich, H.7    Schwarz, H.P.8
  • 39
    • 0027536915 scopus 로고
    • Von Willebrand factor
    • Z. M. Ruggeri, J. Ware. von Willebrand factor. FASEB J. 1993, 7, 308.
    • (1993) FASEB J. , vol.7 , pp. 308
    • Ruggeri, Z.M.1    Ware, J.2
  • 40
    • 0031686041 scopus 로고    scopus 로고
    • Biochemistry and genetics of von Willebrand factor
    • J. E. Sadler. Biochemistry and genetics of von Willebrand factor. Annu. Rev. Biochem. 1998, 67, 395.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 395
    • Sadler, J.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.