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Volumn 356, Issue 1, 2006, Pages 76-85

Simultaneous determination of protein aggregation, degradation, and absolute molecular weight by size exclusion chromatography-multiangle laser light scattering

Author keywords

Absolute molecular weight; Glycoproteins; Pharmaceutical proteins; Protein aggregation; Protein degradation; SEC MALLS

Indexed keywords

ANTIBODIES; BINARY ALLOYS; GLYCOPROTEINS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; LIGHT SCATTERING; MAMMALS; MOLECULAR WEIGHT; REFRACTIVE INDEX; URANIUM ALLOYS; VANADIUM ALLOYS;

EID: 33747175672     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2006.05.025     Document Type: Article
Times cited : (90)

References (37)
  • 3
    • 0036598634 scopus 로고    scopus 로고
    • Bioequivalence and the immunogenicity of biopharmaceuticals
    • Schellekens H. Bioequivalence and the immunogenicity of biopharmaceuticals. Nat. Rev. Drug Discov. 1 (2002) 457-462
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 457-462
    • Schellekens, H.1
  • 5
    • 0033790849 scopus 로고    scopus 로고
    • Formation of disulfide bonds in acid-induced gels of preheated whey protein isolate
    • Alting A.C., Hamer R.J., De Kruif C.G., and Visschers R.W. Formation of disulfide bonds in acid-induced gels of preheated whey protein isolate. J. Agric. Food Chem. 48 (2000) 5001-5007
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 5001-5007
    • Alting, A.C.1    Hamer, R.J.2    De Kruif, C.G.3    Visschers, R.W.4
  • 7
    • 0033822417 scopus 로고    scopus 로고
    • Protection of bovine serum albumin from aggregation by Tween 80
    • Arakawa T., and Kita Y. Protection of bovine serum albumin from aggregation by Tween 80. J. Pharm. Sci. 89 (2000) 646-651
    • (2000) J. Pharm. Sci. , vol.89 , pp. 646-651
    • Arakawa, T.1    Kita, Y.2
  • 8
    • 0027228385 scopus 로고
    • Techniques for assessing the effects of pharmaceutical excipients on the aggregation of porcine growth hormone
    • Charman S.A., Mason K.L., and Charman W.N. Techniques for assessing the effects of pharmaceutical excipients on the aggregation of porcine growth hormone. Pharm. Res. 10 (1993) 954-962
    • (1993) Pharm. Res. , vol.10 , pp. 954-962
    • Charman, S.A.1    Mason, K.L.2    Charman, W.N.3
  • 9
    • 0344413649 scopus 로고    scopus 로고
    • On the oligomeric state of the red blood cell glucose transporter GLUT1
    • Zuo S.S., Hellman U., and Lundahl P. On the oligomeric state of the red blood cell glucose transporter GLUT1. Biochim. Biophys. Acta 1618 (2003) 8-16
    • (2003) Biochim. Biophys. Acta , vol.1618 , pp. 8-16
    • Zuo, S.S.1    Hellman, U.2    Lundahl, P.3
  • 11
    • 0032782071 scopus 로고
    • Instability, stabilization, and formulation of liquid protein pharmaceuticals
    • Wang W. Instability, stabilization, and formulation of liquid protein pharmaceuticals. Int. J. Pharm. 185 (1990) 129-188
    • (1990) Int. J. Pharm. , vol.185 , pp. 129-188
    • Wang, W.1
  • 13
    • 0035013448 scopus 로고    scopus 로고
    • Comparative study of protein molecular weights by size-exclusion chromatography and laser-light scattering
    • Oliva A., Llabres M., and Farina J.B. Comparative study of protein molecular weights by size-exclusion chromatography and laser-light scattering. J. Pharm. Biomed. Anal. 25 (2001) 833-841
    • (2001) J. Pharm. Biomed. Anal. , vol.25 , pp. 833-841
    • Oliva, A.1    Llabres, M.2    Farina, J.B.3
  • 14
    • 0030571043 scopus 로고    scopus 로고
    • Size-exclusion chromatography with on-Line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions
    • Wen J., Arakawa T., and Philo J.S. Size-exclusion chromatography with on-Line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions. Anal. Biochem. 240 (1996) 155-166
    • (1996) Anal. Biochem. , vol.240 , pp. 155-166
    • Wen, J.1    Arakawa, T.2    Philo, J.S.3
  • 15
    • 0001052424 scopus 로고
    • Schuster T.M., and Lave T.M. (Eds), Birkhauser, Boston
    • Shire S.J. In: Schuster T.M., and Lave T.M. (Eds). Modern Analytical Ultracentrifugation (1994), Birkhauser, Boston 261-297
    • (1994) Modern Analytical Ultracentrifugation , pp. 261-297
    • Shire, S.J.1
  • 16
    • 0033152466 scopus 로고    scopus 로고
    • Molecular weights of CTLA-4 and CD80 by sedimentation equilibrium ultracentrifugation
    • Fairman R., Fenderson W., Hail M.E., Wu Y., and Shaw S.Y. Molecular weights of CTLA-4 and CD80 by sedimentation equilibrium ultracentrifugation. Anal. Biochem. 270 (1999) 286-295
    • (1999) Anal. Biochem. , vol.270 , pp. 286-295
    • Fairman, R.1    Fenderson, W.2    Hail, M.E.3    Wu, Y.4    Shaw, S.Y.5
  • 17
    • 0034839464 scopus 로고    scopus 로고
    • Gas-phase binding of non-covalent protein complexes between bovine pancreatic trypsin inhibitor and its target enzymes studied by electrospray ionization tandem mass spectrometry
    • Nesatyy V.J. Gas-phase binding of non-covalent protein complexes between bovine pancreatic trypsin inhibitor and its target enzymes studied by electrospray ionization tandem mass spectrometry. J. Mass Spectrom. 36 (2001) 950-959
    • (2001) J. Mass Spectrom. , vol.36 , pp. 950-959
    • Nesatyy, V.J.1
  • 18
    • 0037111474 scopus 로고    scopus 로고
    • Mass spectrometry evaluation of the solution and gas-phase binding properties of noncovalent protein complexes
    • Nesatyy V.J. Mass spectrometry evaluation of the solution and gas-phase binding properties of noncovalent protein complexes. Int. J. Mass Spectrom. 221 (2002) 147-161
    • (2002) Int. J. Mass Spectrom. , vol.221 , pp. 147-161
    • Nesatyy, V.J.1
  • 19
    • 0017342164 scopus 로고
    • Molecular weights of protein multimers from polyacrylamide gel electrophoresis
    • Bryan J.K. Molecular weights of protein multimers from polyacrylamide gel electrophoresis. Anal. Biochem. 78 (1977) 513-519
    • (1977) Anal. Biochem. , vol.78 , pp. 513-519
    • Bryan, J.K.1
  • 21
    • 0038771206 scopus 로고    scopus 로고
    • Characterization of a polysaccharide-protein complex from Ganoderma tsugae mycelium by size-exclusion chromatography combined with laser light scattering
    • Peng Y., and Zhang L. Characterization of a polysaccharide-protein complex from Ganoderma tsugae mycelium by size-exclusion chromatography combined with laser light scattering. J. Biochem. Biophys. Methods 56 (2003) 243-252
    • (2003) J. Biochem. Biophys. Methods , vol.56 , pp. 243-252
    • Peng, Y.1    Zhang, L.2
  • 23
    • 0042624768 scopus 로고    scopus 로고
    • Analysis of aggregates of human immunoglobulin G using size-exclusion chromatography, static and dynamic light scattering
    • Ahrer K., Buchacher A., Iberer G., Josic D., and Jungbauer A. Analysis of aggregates of human immunoglobulin G using size-exclusion chromatography, static and dynamic light scattering. J. Chromatogr. A 1009 (2003) 89-96
    • (2003) J. Chromatogr. A , vol.1009 , pp. 89-96
    • Ahrer, K.1    Buchacher, A.2    Iberer, G.3    Josic, D.4    Jungbauer, A.5
  • 24
    • 1642456636 scopus 로고    scopus 로고
    • Characterization and analysis of thermal denaturation of antibodies by size exclusion high-performance liquid chromatography with quadruple detection
    • Hartmann W.K., Saptharishi N., Yang X.Y., Mitra G., and Soman G. Characterization and analysis of thermal denaturation of antibodies by size exclusion high-performance liquid chromatography with quadruple detection. Anal. Biochem. 325 (2004) 227-239
    • (2004) Anal. Biochem. , vol.325 , pp. 227-239
    • Hartmann, W.K.1    Saptharishi, N.2    Yang, X.Y.3    Mitra, G.4    Soman, G.5
  • 25
    • 33645074449 scopus 로고    scopus 로고
    • Applications of multi-angle laser light-scattering detection in the analysis of peptides and proteins
    • Oliva A., Llabres M., and Farina J.B. Applications of multi-angle laser light-scattering detection in the analysis of peptides and proteins. Curr. Drug Discov. Technol. 1 (2004) 229-242
    • (2004) Curr. Drug Discov. Technol. , vol.1 , pp. 229-242
    • Oliva, A.1    Llabres, M.2    Farina, J.B.3
  • 26
    • 0642281206 scopus 로고    scopus 로고
    • Use of multi-angle laser light scattering and size-exclusion chromatography to characterize the molecular weight and types of aggregates present in commercial whey protein products
    • Wang T., and Lucey J.A. Use of multi-angle laser light scattering and size-exclusion chromatography to characterize the molecular weight and types of aggregates present in commercial whey protein products. J. Dairy Sci. 86 (2003) 3090-3101
    • (2003) J. Dairy Sci. , vol.86 , pp. 3090-3101
    • Wang, T.1    Lucey, J.A.2
  • 27
    • 0041825189 scopus 로고    scopus 로고
    • Effect of high shear rate on stability of proteins: kinetic study
    • Oliva A., Santovena A., Farina J., and Llabres M. Effect of high shear rate on stability of proteins: kinetic study. J. Pharm. Biomed. Anal. 33 (2003) 145-155
    • (2003) J. Pharm. Biomed. Anal. , vol.33 , pp. 145-155
    • Oliva, A.1    Santovena, A.2    Farina, J.3    Llabres, M.4
  • 28
    • 0027498262 scopus 로고
    • Light scattering and the absolute characterization of macromolecules
    • Wyatt P.J. Light scattering and the absolute characterization of macromolecules. Anal. Chim. Acta 272 (1993) 1-40
    • (1993) Anal. Chim. Acta , vol.272 , pp. 1-40
    • Wyatt, P.J.1
  • 29
    • 0035894420 scopus 로고    scopus 로고
    • Online size-exclusion high-performance liquid chromatography light scattering and differential refractometry methods to determine degree of polymer conjugation to proteins and protein-protein or protein-ligand association states
    • Kendrick B.S., Kerwin B.A., Chang B.S., and Philo J.S. Online size-exclusion high-performance liquid chromatography light scattering and differential refractometry methods to determine degree of polymer conjugation to proteins and protein-protein or protein-ligand association states. Anal. Biochem. 299 (2001) 136-146
    • (2001) Anal. Biochem. , vol.299 , pp. 136-146
    • Kendrick, B.S.1    Kerwin, B.A.2    Chang, B.S.3    Philo, J.S.4
  • 30
    • 0004250290 scopus 로고    scopus 로고
    • Electrophoresis
    • Coligan J.E., Dunn B.M., Speicher D.W., and Wingfield P.T. (Eds), Wiley, New York
    • Speicher D.W. Electrophoresis. In: Coligan J.E., Dunn B.M., Speicher D.W., and Wingfield P.T. (Eds). Current Protocols in Protein Science (1999), Wiley, New York
    • (1999) Current Protocols in Protein Science
    • Speicher, D.W.1
  • 32
    • 0024861466 scopus 로고
    • Characterization of biopolymers using a multi angle light scattering detector with size exclusion chromatography
    • Jackson C., Nilsson L.M., and Wyatt P.J. Characterization of biopolymers using a multi angle light scattering detector with size exclusion chromatography. J. Appl. Polymer Sci. Appl. Polymer Symp. 99 (1989) 99-114
    • (1989) J. Appl. Polymer Sci. Appl. Polymer Symp. , vol.99 , pp. 99-114
    • Jackson, C.1    Nilsson, L.M.2    Wyatt, P.J.3
  • 33
    • 0030043206 scopus 로고    scopus 로고
    • Proteins in frozen solutions: evidence of ice-induced partial unfolding
    • Strambini G.B., and Gabellieri E. Proteins in frozen solutions: evidence of ice-induced partial unfolding. Biophys. J. 70 (1996) 971-976
    • (1996) Biophys. J. , vol.70 , pp. 971-976
    • Strambini, G.B.1    Gabellieri, E.2
  • 34
    • 0031660957 scopus 로고    scopus 로고
    • Effects of Tween 80 and sucrose on acute short-term stablity and long-term storage at -20 °C of a recombinant hemoglobin
    • Kerwin B.A., Heller M.C., Levin S.H., and Randolph T.W. Effects of Tween 80 and sucrose on acute short-term stablity and long-term storage at -20 °C of a recombinant hemoglobin. J. Pharm. Sci. 87 (1998) 1062-1068
    • (1998) J. Pharm. Sci. , vol.87 , pp. 1062-1068
    • Kerwin, B.A.1    Heller, M.C.2    Levin, S.H.3    Randolph, T.W.4
  • 35
    • 33747181260 scopus 로고    scopus 로고
    • Reopro online, description, chemistry, ingredients-Abciximab-RxList monographs. (accessed 3-3-2006). Ref type: electronic citation.
  • 36
    • 33747171334 scopus 로고    scopus 로고
    • GAPDH as a loading control in Western blotting. (accessed 3-3-2006). Ref type: electronic citation.
  • 37
    • 0028816796 scopus 로고
    • Stability of protein formulations: Investigation of surfactant effects by a novel EPR spectroscopic technique
    • Bam N.B., Randolph T.W., and Cleland J.L. Stability of protein formulations: Investigation of surfactant effects by a novel EPR spectroscopic technique. Pharm. Res. 12 (1995) 2-11
    • (1995) Pharm. Res. , vol.12 , pp. 2-11
    • Bam, N.B.1    Randolph, T.W.2    Cleland, J.L.3


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