메뉴 건너뛰기




Volumn 93, Issue 6, 2004, Pages 1390-1402

Challenges in the development of high protein concentration formulations

Author keywords

Analytical; High concentration; Manufacturing; Pharmaceutical; Protein formulation; Viscosity

Indexed keywords

PROTEIN; RITUXIMAB; TRASTUZUMAB;

EID: 2642550862     PISSN: 00223549     EISSN: None     Source Type: Journal    
DOI: 10.1002/jps.20079     Document Type: Short Survey
Times cited : (772)

References (71)
  • 3
    • 0025218116 scopus 로고
    • Solubility as a function of protein structure and solvent components
    • Schein CH. 1990. Solubility as a function of protein structure and solvent components. BioTechnol 8(4):308-317.
    • (1990) BioTechnol , vol.8 , Issue.4 , pp. 308-317
    • Schein, C.H.1
  • 4
    • 0017623134 scopus 로고
    • Salt effect on hydrophobic interactions in precipitation and chromatography of proteins: An interpretation of the lyotropic series
    • Melander W, Horvath C. 1977. Salt effect on hydrophobic interactions in precipitation and chromatography of proteins: An interpretation of the lyotropic series. Arch Biochem Biophys 183(1):200-215.
    • (1977) Arch Biochem Biophys , vol.183 , Issue.1 , pp. 200-215
    • Melander, W.1    Horvath, C.2
  • 5
    • 0031892702 scopus 로고    scopus 로고
    • Three solutions of the protein solubility problem
    • Jenkins WT. 1998. Three solutions of the protein solubility problem. Protein Sci 7(2):376-382.
    • (1998) Protein Sci , vol.7 , Issue.2 , pp. 376-382
    • Jenkins, W.T.1
  • 6
    • 0016160230 scopus 로고
    • The solubility of fibrinogen in dilute salt solutions
    • Leavis PC, Rothstein F. 1974. The solubility of fibrinogen in dilute salt solutions. Arch Biochem Biophys 161(2):671-682.
    • (1974) Arch Biochem Biophys , vol.161 , Issue.2 , pp. 671-682
    • Leavis, P.C.1    Rothstein, F.2
  • 7
    • 0001635487 scopus 로고    scopus 로고
    • A micromethod for concentration and desalting utilizing a hollow fiber with special reference to capillary electrophoresis
    • Zhang R, Hjerten S. 1997. A micromethod for concentration and desalting utilizing a hollow fiber with special reference to capillary electrophoresis. Anal Chem 69(8):1585-1592.
    • (1997) Anal Chem , vol.69 , Issue.8 , pp. 1585-1592
    • Zhang, R.1    Hjerten, S.2
  • 8
    • 0021424329 scopus 로고
    • A rapid method of concentrating proteins in small volumes with high recovery using Sephadex G-25
    • Saul A, Don M. 1984. A rapid method of concentrating proteins in small volumes with high recovery using Sephadex G-25. Anal Biochem 138(2):451-453.
    • (1984) Anal Biochem , vol.138 , Issue.2 , pp. 451-453
    • Saul, A.1    Don, M.2
  • 10
    • 0028312873 scopus 로고
    • Differential precipitation of proteins. Science and technology
    • Rothstein F. 1994. Differential precipitation of proteins. Science and technology. Bioprocess Technol 18:115-208.
    • (1994) Bioprocess Technol , vol.18 , pp. 115-208
    • Rothstein, F.1
  • 11
    • 0034278161 scopus 로고    scopus 로고
    • Producing a low ovomucoid egg white preparation by precipitation with aqueous ethanol
    • Tanabe S, Tesaki S, Watanabe M. 2000. Producing a low ovomucoid egg white preparation by precipitation with aqueous ethanol. Biosc Biotechnol Biochem 64(9):2005-2007.
    • (2000) Biosc Biotechnol Biochem , vol.64 , Issue.9 , pp. 2005-2007
    • Tanabe, S.1    Tesaki, S.2    Watanabe, M.3
  • 12
    • 0011673651 scopus 로고
    • Modeling of aggregation-precipitation phenomena
    • Ahern TJ, Manning MC, editors, New York: Plenum Press
    • Glatz CE. 1992. Modeling of aggregation-precipitation phenomena. In: Ahern TJ, Manning MC, editors. Stability of protein pharmaceuticals, 1st edn., New York: Plenum Press. p 135-166.
    • (1992) Stability of Protein Pharmaceuticals, 1st Edn. , pp. 135-166
    • Glatz, C.E.1
  • 13
    • 0345701503 scopus 로고    scopus 로고
    • Supercritical fluid processing of proteins: Lysozyme precipitation from aqueous solution
    • Moshashaee S, Bisrat M, Forbes RT, Quinn EA, Nyqvist H, York P. 2003. Supercritical fluid processing of proteins: Lysozyme precipitation from aqueous solution. J Pharm Pharmacol 55(2): 185-192.
    • (2003) J Pharm Pharmacol , vol.55 , Issue.2 , pp. 185-192
    • Moshashaee, S.1    Bisrat, M.2    Forbes, R.T.3    Quinn, E.A.4    Nyqvist, H.5    York, P.6
  • 15
    • 0036250675 scopus 로고    scopus 로고
    • Freezing bulk-scale biopharmaceuticals using common techniques-And the magnitude of freeze-concentration
    • Webb SD, Webb JN, Hughes TG, Sesin DF, Kincaid AC. 2002. Freezing bulk-scale biopharmaceuticals using common techniques-And the magnitude of freeze-concentration. Biopharm 15(5):2-8.
    • (2002) Biopharm , vol.15 , Issue.5 , pp. 2-8
    • Webb, S.D.1    Webb, J.N.2    Hughes, T.G.3    Sesin, D.F.4    Kincaid, A.C.5
  • 17
    • 0024806396 scopus 로고
    • Stability of protein pharmaceuticals
    • Manning MC, Patel K, Borchardt RT. 1989. Stability of protein pharmaceuticals. Pharm Res 6(11):903-918.
    • (1989) Pharm Res , vol.6 , Issue.11 , pp. 903-918
    • Manning, M.C.1    Patel, K.2    Borchardt, R.T.3
  • 18
    • 0027729733 scopus 로고
    • The development of stable protein formulations: A close look at protein aggregation, deamidation and oxidation
    • Cleland JL, Powell MF, Shire SJ. 1993. The development of stable protein formulations: A close look at protein aggregation, deamidation and oxidation. Crit Rev Ther Drug Carrier Syst 10(4):307-377.
    • (1993) Crit Rev Ther Drug Carrier Syst , vol.10 , Issue.4 , pp. 307-377
    • Cleland, J.L.1    Powell, M.F.2    Shire, S.J.3
  • 19
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in non-native protein aggregation
    • Chi EY, Krishnan S, Randolph TW, Carpenter JF. 2003. Physical stability of proteins in aqueous solution: Mechanism and driving forces in non-native protein aggregation. Pharm Res 20(9):1325-1336.
    • (2003) Pharm Res , vol.20 , Issue.9 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 20
    • 0036111474 scopus 로고    scopus 로고
    • Inverse relationship of protein concentration and aggregation
    • Treuheit MJ, Kosky AA, Brems DN. 2002. Inverse relationship of protein concentration and aggregation. Pharm Res 19(4):511-516.
    • (2002) Pharm Res , vol.19 , Issue.4 , pp. 511-516
    • Treuheit, M.J.1    Kosky, A.A.2    Brems, D.N.3
  • 21
    • 0030856842 scopus 로고    scopus 로고
    • Protein aggregates seem to play a key role among the parameters influencing the antigenicity of interferon alpha (IFN-alpha) in normal and transgenic mice
    • Braun A, Kwee L, Labow MA, Alsenz J. 1997. Protein aggregates seem to play a key role among the parameters influencing the antigenicity of interferon alpha (IFN-alpha) in normal and transgenic mice. Pharm Res 14(10):1472-1478.
    • (1997) Pharm Res , vol.14 , Issue.10 , pp. 1472-1478
    • Braun, A.1    Kwee, L.2    Labow, M.A.3    Alsenz, J.4
  • 22
    • 0036890997 scopus 로고    scopus 로고
    • Immune responses to therapeutic proteins in humans-Clinical significance, assessment and prediction
    • Koren E, Zuckerman LA, Mire-Sluis AR. 2002. Immune responses to therapeutic proteins in humans-Clinical significance, assessment and prediction. Curr Pharm Biotechnol 3(4):349-360.
    • (2002) Curr Pharm Biotechnol , vol.3 , Issue.4 , pp. 349-360
    • Koren, E.1    Zuckerman, L.A.2    Mire-Sluis, A.R.3
  • 23
    • 0026730739 scopus 로고
    • Confinement as a determinant of macromolecular structure and reactivity
    • Minton AP. 1992. Confinement as a determinant of macromolecular structure and reactivity. Biophysical J 63(4):1090-1100.
    • (1992) Biophysical J , vol.63 , Issue.4 , pp. 1090-1100
    • Minton, A.P.1
  • 24
    • 0019890347 scopus 로고
    • Evidence for protein self-association induced by excluded volume. Myoglobin in the presence of globular proteins
    • Wilf J, Minton AP. 1981. Evidence for protein self-association induced by excluded volume. Myoglobin in the presence of globular proteins. Biochimica et Biophysica Acta 670(3):316-322.
    • (1981) Biochimica et Biophysica Acta , vol.670 , Issue.3 , pp. 316-322
    • Wilf, J.1    Minton, A.P.2
  • 25
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biochemical, biophysical, and physiological consequences
    • Zimmerman SB, Minton AP. 1993. Macromolecular crowding: Biochemical, biophysical, and physiological consequences. Annu Rev Biophys Biomol Struct 22:27-65.
    • (1993) Annu Rev Biophys Biomol Struct , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2
  • 27
    • 0020477017 scopus 로고
    • Stabilization of protein structure by sugars
    • Arakawa T, Timasheff SN. 1982. Stabilization of protein structure by sugars. Biochemistry 21:6536-6544.
    • (1982) Biochemistry , vol.21 , pp. 6536-6544
    • Arakawa, T.1    Timasheff, S.N.2
  • 28
    • 0025732448 scopus 로고
    • Protein-solvent interactions in pharmaceutical formulations
    • Arakawa T, Kita Y, Carpenter JF. 1991. Protein-solvent interactions in pharmaceutical formulations. Pharm Res 8(3):285-291.
    • (1991) Pharm Res , vol.8 , Issue.3 , pp. 285-291
    • Arakawa, T.1    Kita, Y.2    Carpenter, J.F.3
  • 29
    • 0003220389 scopus 로고
    • Freeze-drying of proteins: Process, formulation and stability
    • Cleland JL, Langer R, editors, Washington D.C.: American Chemical Society
    • Pikal MJ. 1994. Freeze-drying of proteins: Process, formulation and stability. In: Cleland JL, Langer R, editors. Formulation and delivery of proteins and peptides, 1st edn., Washington D.C.: American Chemical Society. p 120-133.
    • (1994) Formulation and Delivery of Proteins and Peptides, 1st Edn. , pp. 120-133
    • Pikal, M.J.1
  • 30
    • 55449104956 scopus 로고    scopus 로고
    • Mechanisms of aggregate formation and carbohydrate excipient stabilization of lyophilized humanized monoclonal antibody formulations
    • Andya JD, Hsu CC, Shire SJ. 2003. Mechanisms of aggregate formation and carbohydrate excipient stabilization of lyophilized humanized monoclonal antibody formulations. Aaps Pharmsci 5(2):E10.
    • (2003) Aaps Pharmsci , vol.5 , Issue.2
    • Andya, J.D.1    Hsu, C.C.2    Shire, S.J.3
  • 31
    • 0030770631 scopus 로고    scopus 로고
    • Rational design of stable lyophilized protein formulations: Some practical advice
    • Carpenter JF, Pikal MJ, Chang BS, Randolph TW. 1997. Rational design of stable lyophilized protein formulations: Some practical advice. Pharm Res 14(8):969-975.
    • (1997) Pharm Res , vol.14 , Issue.8 , pp. 969-975
    • Carpenter, J.F.1    Pikal, M.J.2    Chang, B.S.3    Randolph, T.W.4
  • 34
    • 0020758702 scopus 로고
    • Several uses for tangential-flow filtration in the pharmaceutical industry
    • Genovesi CS. 1983. Several uses for tangential-flow filtration in the pharmaceutical industry. J Parenter Sci Technol 37(3):81-86.
    • (1983) J Parenter Sci Technol , vol.37 , Issue.3 , pp. 81-86
    • Genovesi, C.S.1
  • 36
    • 0035313212 scopus 로고    scopus 로고
    • Membrane separations in biotechnology
    • van Reis R, Zydney A. 2001. Membrane separations in biotechnology. Curr Opin Biotechnol 12(2):208-211.
    • (2001) Curr Opin Biotechnol , vol.12 , Issue.2 , pp. 208-211
    • Van Reis, R.1    Zydney, A.2
  • 37
    • 0018599354 scopus 로고
    • Action of shear on enzymes: Studies with alcohol dehydrogenase
    • Thomas CR, Nienow AW, Dunnill P. 1979. Action of shear on enzymes: Studies with alcohol dehydrogenase. Biotechnol Bioeng 21(12):2263-2278.
    • (1979) Biotechnol Bioeng , vol.21 , Issue.12 , pp. 2263-2278
    • Thomas, C.R.1    Nienow, A.W.2    Dunnill, P.3
  • 38
    • 0016169554 scopus 로고
    • Shear-induced protein-protein interaction at the air-water interface
    • Watterson JG, Schaub MC, Waser PG. 1974. Shear-induced protein-protein interaction at the air-water interface. Biochimica et Biophysica Acta 356(2):133-143.
    • (1974) Biochimica et Biophysica Acta , vol.356 , Issue.2 , pp. 133-143
    • Watterson, J.G.1    Schaub, M.C.2    Waser, P.G.3
  • 39
    • 0032210795 scopus 로고    scopus 로고
    • Comparison of ultra- and microfiltration in the presence and absence of secondary flow with polysaccharides, proteins, and yeast suspensions
    • Gehlert G, Luque S, Belfort G. 1998. Comparison of ultra- and microfiltration in the presence and absence of secondary flow with polysaccharides, proteins, and yeast suspensions. Biotechnol Progress 14(6):931-942.
    • (1998) Biotechnol Progress , vol.14 , Issue.6 , pp. 931-942
    • Gehlert, G.1    Luque, S.2    Belfort, G.3
  • 41
    • 2642518786 scopus 로고    scopus 로고
    • Biotechnology-based pharmaceuticals
    • Banker GS, Rhodes CT, editors, New York: Marcel Dekker
    • Rouan SKE. 1996. Biotechnology-based pharmaceuticals. In: Banker GS, Rhodes CT, editors. Modern pharmaceutics, 3rd edn., New York: Marcel Dekker. p 843-873.
    • (1996) Modern Pharmaceutics, 3rd Edn. , pp. 843-873
    • Rouan, S.K.E.1
  • 42
    • 0028389661 scopus 로고
    • Fluid bed drying in the laboratory
    • Poupitch G. 1994. Fluid bed drying in the laboratory. Am Biotechnol Lab 12(4):30-34.
    • (1994) Am Biotechnol Lab , vol.12 , Issue.4 , pp. 30-34
    • Poupitch, G.1
  • 43
    • 0036278010 scopus 로고    scopus 로고
    • Accelerated fluid bed drying using NIR monitoring and phenomenological modeling: Method assessment and formulation suitability
    • Wildfong PL, Samy AS, Corfa J, Peck GE, Morris KR. 2002. Accelerated fluid bed drying using NIR monitoring and phenomenological modeling: Method assessment and formulation suitability. J Pharm Sci 91(3):631-639.
    • (2002) J Pharm Sci , vol.91 , Issue.3 , pp. 631-639
    • Wildfong, P.L.1    Samy, A.S.2    Corfa, J.3    Peck, G.E.4    Morris, K.R.5
  • 44
    • 0032899267 scopus 로고    scopus 로고
    • Formulation of proteins in vacuum-dried glasses. II. Process and storage stability in sugar-free amino acid systems
    • Mattern M, Winter G, Kohnert U, Lee G. 1999. Formulation of proteins in vacuum-dried glasses. II. Process and storage stability in sugar-free amino acid systems. Pharm Dev Technol 4(2):199-208.
    • (1999) Pharm Dev Technol , vol.4 , Issue.2 , pp. 199-208
    • Mattern, M.1    Winter, G.2    Kohnert, U.3    Lee, G.4
  • 45
    • 0031660286 scopus 로고    scopus 로고
    • Stabilization of lactate dehydrogenase following freeze thawing and vacuum-drying in the presence of trehalose and borate
    • Miller DP, Anderson RE, de Pablo JJ. 1998. Stabilization of lactate dehydrogenase following freeze thawing and vacuum-drying in the presence of trehalose and borate. Pharm Res 15(8):1215-1221.
    • (1998) Pharm Res , vol.15 , Issue.8 , pp. 1215-1221
    • Miller, D.P.1    Anderson, R.E.2    De Pablo, J.J.3
  • 46
    • 0346637757 scopus 로고
    • Parenteral preparations
    • Gennaro AR, editor, Easton, PA: Mack Publishing Company
    • Avis KE. 1990. Parenteral preparations. In: Gennaro AR, editor Remington's pharmaceutical sciences, 18th edn., Easton, PA: Mack Publishing Company. p 1545-1569.
    • (1990) Remington's Pharmaceutical Sciences, 18th Edn. , pp. 1545-1569
    • Avis, K.E.1
  • 47
    • 0028846780 scopus 로고
    • Crystallization of intact monoclonal antibodies
    • Harris LJ, Skaletsky E, McPherson A. 1995. Crystallization of intact monoclonal antibodies. Proteins 23(2):285-289.
    • (1995) Proteins , vol.23 , Issue.2 , pp. 285-289
    • Harris, L.J.1    Skaletsky, E.2    McPherson, A.3
  • 49
    • 0009359412 scopus 로고    scopus 로고
    • Formulation and administration techniques to minimize injection pain and tissue dammage associated with parenteral products
    • Gapta PK, Brazeau GA, editors, Denver: Interpharm Press
    • Gatlin LA, Gatlin CAB. 1999. Formulation and administration techniques to minimize injection pain and tissue dammage associated with parenteral products. In: Gapta PK, Brazeau GA, editors. Injectable drug development: Techniques to reduce pain and irritation, 1st edn., Denver: Interpharm Press. p 401-421.
    • (1999) Injectable Drug Development: Techniques to Reduce Pain and Irritation, 1st Edn. , pp. 401-421
    • Gatlin, L.A.1    Gatlin, C.A.B.2
  • 50
    • 0006090244 scopus 로고
    • Analytical methods for the assessment of protein formulations and delivery systems
    • Cleland JL, Langer R, editors, Washington D.C.: American Chemical Society
    • Jones AJS. 1993. Analytical methods for the assessment of protein formulations and delivery systems. In: Cleland JL, Langer R, editors. Formulation and delivery of peptides and proteins, 1st edn., Washington D.C.: American Chemical Society. p 22-45.
    • (1993) Formulation and Delivery of Peptides and Proteins, 1st Edn. , pp. 22-45
    • Jones, A.J.S.1
  • 52
    • 2642574201 scopus 로고
    • International symposium on biological product freeze-drying and formulation
    • Hatley RHM. 1990. International symposium on biological product freeze-drying and formulation, Bethesda MD. p 105-122.
    • (1990) Bethesda MD , pp. 105-122
    • Hatley, R.H.M.1
  • 53
    • 0034854492 scopus 로고    scopus 로고
    • Effect of moisture on the stability of a lyophilized humanized monoclonal antibody formulation
    • Breen ED, Curley JG, Overcashier DE, Hsu CC, Shire SJ. 2001. Effect of moisture on the stability of a lyophilized humanized monoclonal antibody formulation. Pharm Res 18(9):1345-1353.
    • (2001) Pharm Res , vol.18 , Issue.9 , pp. 1345-1353
    • Breen, E.D.1    Curley, J.G.2    Overcashier, D.E.3    Hsu, C.C.4    Shire, S.J.5
  • 54
    • 0033025193 scopus 로고    scopus 로고
    • Characterization of the glass transition of HPMC using modulated differential scanning calorimetry
    • McPhillips H, Craig DQ, Royall PG, Hill VL. 1999. Characterization of the glass transition of HPMC using modulated differential scanning calorimetry. Int J Pharm 180:83-90.
    • (1999) Int J Pharm , vol.180 , pp. 83-90
    • McPhillips, H.1    Craig, D.Q.2    Royall, P.G.3    Hill, V.L.4
  • 55
    • 0031695133 scopus 로고    scopus 로고
    • Fourier-transform infrared spectroscopic investigation of the secondary structure of aqueous and dried recombinant human deoxyribonuclease I
    • Costantino HR, Chen B, Griebenow K, Hsu CC, Shire SJ. 1998. Fourier-transform infrared spectroscopic investigation of the secondary structure of aqueous and dried recombinant human deoxyribonuclease I. Pharm Pharmacol Commun 4:391-395.
    • (1998) Pharm Pharmacol Commun , vol.4 , pp. 391-395
    • Costantino, H.R.1    Chen, B.2    Griebenow, K.3    Hsu, C.C.4    Shire, S.J.5
  • 56
    • 0027163348 scopus 로고
    • Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers
    • Prestrelski SJ, Tedeschi N, Arakawa T, Carpenter JF. 1993. Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers. Biophysical J 65(2):661-671.
    • (1993) Biophysical J , vol.65 , Issue.2 , pp. 661-671
    • Prestrelski, S.J.1    Tedeschi, N.2    Arakawa, T.3    Carpenter, J.F.4
  • 57
    • 0037382047 scopus 로고    scopus 로고
    • Steady-state trytophan fluorescence spectrscopy study to probe tertiary structure of proteins in solid powders
    • Sharma VK, Kalonia DS. 2003. Steady-state trytophan fluorescence spectrscopy study to probe tertiary structure of proteins in solid powders. J Pharm Sci 92(4):890-899.
    • (2003) J Pharm Sci , vol.92 , Issue.4 , pp. 890-899
    • Sharma, V.K.1    Kalonia, D.S.2
  • 58
    • 0001052424 scopus 로고
    • Analytical ultracentrifugation and its use in biotechnology
    • Schuster TM, Laue TM, editors, Boston: Birkhauser
    • Shire SJ. 1992. Analytical ultracentrifugation and its use in biotechnology. In: Schuster TM, Laue TM, editors. Modern analytical ultracentrifugation, 1st edn., Boston: Birkhauser. p 261-297.
    • (1992) Modern Analytical Ultracentrifugation, 1st Edn. , pp. 261-297
    • Shire, S.J.1
  • 59
    • 0036707991 scopus 로고    scopus 로고
    • Modern analytical ultracentrifugation in protein science: A tutorial review
    • Lebowitz J, Lewis MS, Schuck P. 2002. Modern analytical ultracentrifugation in protein science: A tutorial review. Protein Sci 11(9):2067-2079.
    • (2002) Protein Sci , vol.11 , Issue.9 , pp. 2067-2079
    • Lebowitz, J.1    Lewis, M.S.2    Schuck, P.3
  • 60
    • 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, Philo JS. 1996. Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions. Anal Biochem 240(2):155-166.
    • (1996) Anal Biochem , vol.240 , Issue.2 , pp. 155-166
    • Wen, J.1    Arakawa, T.2    Philo, J.S.3
  • 61
    • 0345426282 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of dimer formation and dissociation for a recombinant humanized monoclonal antibody to vascular endothelial growth factor
    • Moore JM, Patapoff TW, Cromwell ME. 1999. Kinetics and thermodynamics of dimer formation and dissociation for a recombinant humanized monoclonal antibody to vascular endothelial growth factor. Biochemistry 38(42):13960-13967.
    • (1999) Biochemistry , vol.38 , Issue.42 , pp. 13960-13967
    • Moore, J.M.1    Patapoff, T.W.2    Cromwell, M.E.3
  • 62
    • 0019349226 scopus 로고
    • Quasi-elastic light scattering applications in biochemistry and biology
    • Bloomfield VA. 1981. Quasi-elastic light scattering applications in biochemistry and biology. Annu Rev Biophys Bioeng 10:421-450.
    • (1981) Annu Rev Biophys Bioeng , vol.10 , pp. 421-450
    • Bloomfield, V.A.1
  • 63
    • 0033251227 scopus 로고    scopus 로고
    • Light scattering studies on supersaturated protein solutions
    • Georgalis Y, Saenger W. 1999. Light scattering studies on supersaturated protein solutions. Sci Progress 82(Pt. 4):271-294.
    • (1999) Sci Progress , vol.82 , Issue.PART 4 , pp. 271-294
    • Georgalis, Y.1    Saenger, W.2
  • 64
    • 0015457756 scopus 로고
    • Quasi-elastic light scattering from macromolecules
    • Pecora R. 1972. Quasi-elastic light scattering from macromolecules. Annu Rev Biophys Bioeng 1:257-276.
    • (1972) Annu Rev Biophys Bioeng , vol.1 , pp. 257-276
    • Pecora, R.1
  • 65
    • 0017555826 scopus 로고
    • Dynamic light scattering of biopolymers and biocolloids
    • Schurr JM. 1977. Dynamic light scattering of biopolymers and biocolloids. CRC Crit Rev Biochem 4(4):371-431.
    • (1977) CRC Crit Rev Biochem , vol.4 , Issue.4 , pp. 371-431
    • Schurr, J.M.1
  • 66
    • 0024615169 scopus 로고
    • Analytical centrifugation with preparative ultracentrifuges
    • Minton AP. 1989. Analytical centrifugation with preparative ultracentrifuges. Anal Biochem 176:209-216.
    • (1989) Anal Biochem , vol.176 , pp. 209-216
    • Minton, A.P.1
  • 67
    • 0003060984 scopus 로고
    • Comments on the analysis of sedimentation equilibrium experiments
    • Schuster TM, Laue TM, editors, Boston: Birkhauser
    • Johnson ML, Straume M. 1994. Comments on the analysis of sedimentation equilibrium experiments. In: Schuster TM, Laue TM, editors. Modern analytical ultracentrifugation, 1st edn., Boston: Birkhauser. p 37-63.
    • (1994) Modern Analytical Ultracentrifugation, 1st Edn. , pp. 37-63
    • Johnson, M.L.1    Straume, M.2
  • 68
    • 0031688168 scopus 로고    scopus 로고
    • Sedimentation analysis of non-interacting and self-associating solutes using numerical solutions to the Lamm equation
    • Schuck P. 1998. Sedimentation analysis of non-interacting and self-associating solutes using numerical solutions to the Lamm equation. Biophys J 75(3):1503-1512.
    • (1998) Biophys J , vol.75 , Issue.3 , pp. 1503-1512
    • Schuck, P.1
  • 69
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems
    • Schuck P, Perugini MA, Gonzales NR, Howlett GJ, Schubert D. 2002. Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems. Biophys J 82(2):1096-1111.
    • (2002) Biophys J , vol.82 , Issue.2 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Howlett, G.J.4    Schubert, D.5
  • 70
    • 0002033301 scopus 로고
    • Sedimentation coefficients of complex biological particles
    • Harding SE, Rowe AJ, Horton JC, editors, Cambridge, England: The Royal Society of Chemistry
    • de la Torre JG. 1992. Sedimentation coefficients of complex biological particles. In: Harding SE, Rowe AJ, Horton JC, editors. Analytical ultracentrifugation in biochemistry and polymer science, 1st edn., Cambridge, England: The Royal Society of Chemistry. p 333-345.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science, 1st Edn. , pp. 333-345
    • De La Torre, J.G.1
  • 71
    • 0029117815 scopus 로고
    • Characterization of complex formation by humanized anti-IgE monoclonal antibody and monoclonal human IgE
    • Liu J, Lester P, Builder S, Shire SJ. 1995. Characterization of complex formation by humanized anti-IgE monoclonal antibody and monoclonal human IgE. Biochemistry 34(33):10474-10482.
    • (1995) Biochemistry , vol.34 , Issue.33 , pp. 10474-10482
    • Liu, J.1    Lester, P.2    Builder, S.3    Shire, S.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.