메뉴 건너뛰기




Volumn , Issue , 2010, Pages 257-299

Approaches to Control Protein Aggregation during Bulk Production

Author keywords

Biological protein pharmaceutics class of therapeutics, high specificity, unique mechanism of action; Protein aggregation control approaches and bulk production; Protein folding, complex series of equilibria balancing unfolded, intermediate, native, and aggregated states

Indexed keywords


EID: 84886072770     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470769829.ch6     Document Type: Chapter
Times cited : (10)

References (62)
  • 1
    • 84886028357 scopus 로고    scopus 로고
    • FDA guidance concerning demonstration of comparability of human biological products including therapeutic biotechnology-derived products Center for Biologics Evaluation and Research and Center for Drug Evaluation and Research
    • April
    • FDA guidance concerning demonstration of comparability of human biological products, including therapeutic biotechnology-derived products, Center for Biologics Evaluation and Research and Center for Drug Evaluation and Research. April, 1996.
    • (1996)
  • 3
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: An immunologic perspective
    • Rosenberg AS. 2006. Effects of protein aggregates: An immunologic perspective. AAPS J 8: 501-507.
    • (2006) AAPS J , vol.8 , pp. 501-507
    • Rosenberg, A.S.1
  • 5
    • 0024412497 scopus 로고
    • Mutational effects on protein stability
    • Alber T. 1989. Mutational effects on protein stability. Annu Rev Biochem 58: 765-798.
    • (1989) Annu Rev Biochem , vol.58 , pp. 765-798
    • Alber, T.1
  • 7
    • 33846420459 scopus 로고
    • Engineering dramatic increases in the stability of subtilisin
    • In Ahern TJ, Manning MC, eds., Stability of Protein Pharmaceuticals, Vol. B. New York: Plenum Press
    • Bryan PN. 1992. Engineering dramatic increases in the stability of subtilisin. In Ahern TJ, Manning MC, eds., Stability of Protein Pharmaceuticals, Vol. B. New York: Plenum Press.
    • (1992)
    • Bryan, P.N.1
  • 8
    • 84885988690 scopus 로고    scopus 로고
    • Assessment of manufacturability of protein drug candidates by ranking of antibody candidates based on accelerated stability studies
    • 236th ACS National Meeting Division of Biochemical Technology BIOT120 Philadelphia PA
    • Hathway K, Gao S, Salmeron L, Chang J, Buko A. 2008. Assessment of manufacturability of protein drug candidates by ranking of antibody candidates based on accelerated stability studies. 236th ACS National Meeting, Division of Biochemical Technology, BIOT120, Philadelphia, PA, p. 52.
    • (2008) , pp. 52
    • Hathway, K.1    Gao, S.2    Salmeron, L.3    Chang, J.4    Buko, A.5
  • 9
    • 84886077053 scopus 로고    scopus 로고
    • Manufacturability assessments for early stage therapeutic candidate screenings
    • Presented at the IBC BPI Meeting Anaheim CA
    • Ramachander R. 2008. Manufacturability assessments for early stage therapeutic candidate screenings. Presented at the IBC BPI Meeting, Anaheim, CA.
    • (2008)
    • Ramachander, R.1
  • 10
    • 84885971909 scopus 로고    scopus 로고
    • Manufacturability assessment for a successful therapeutic product
    • 236th ACS National Meeting Division of Biochemical Technology BIOT110 Philadelphia PA
    • Jiang Y, Ramachander R, Wen J, Li C, Li J, Angell N, Bondarenco P, Narhi L. 2008. Manufacturability assessment for a successful therapeutic product. 236th ACS National Meeting, Division of Biochemical Technology, BIOT110, Philadelphia, PA, p. 49.
    • (2008) , pp. 49
    • Jiang, Y.1    Ramachander, R.2    Wen, J.3    Li, C.4    Li, J.5    Angell, N.6    Bondarenco, P.7    Narhi, L.8
  • 11
    • 55749103567 scopus 로고    scopus 로고
    • Applications of DSC for antibodies and Fc-conjugated proteins
    • Wen J, Jiang Y, Narhi L. 2007. Applications of DSC for antibodies and Fc-conjugated proteins. Am Pharm Rev 10: 10-15.
    • (2007) Am Pharm Rev , vol.10 , pp. 10-15
    • Wen, J.1    Jiang, Y.2    Narhi, L.3
  • 12
    • 84871292580 scopus 로고    scopus 로고
    • Using differential scanning calorimetry in understanding the correlation between thermal stability and protein stability
    • MicroCal Application Note
    • Wen J, Jiang Y, Hymes K, Gong K, Narhi L. 2007. Using differential scanning calorimetry in understanding the correlation between thermal stability and protein stability. MicroCal Application Note.
    • (2007)
    • Wen, J.1    Jiang, Y.2    Hymes, K.3    Gong, K.4    Narhi, L.5
  • 15
    • 4043131516 scopus 로고    scopus 로고
    • Stability of enzymes and proteins in dried glassy systems: Effect of simulated sunlight conditions
    • Espinosa L, Schebor C, Nudelman NS, Chirife J. 2004. Stability of enzymes and proteins in dried glassy systems: Effect of simulated sunlight conditions. Biotechnol Prog 20 (4): 1220-1224.
    • (2004) Biotechnol Prog , vol.20 , Issue.4 , pp. 1220-1224
    • Espinosa, L.1    Schebor, C.2    Nudelman, N.S.3    Chirife, J.4
  • 16
    • 8344271026 scopus 로고    scopus 로고
    • Production of recombinant proteins in cultivated mammalian cells
    • Wurm FM. 2004. Production of recombinant proteins in cultivated mammalian cells. Nat Biotechnol 22 (11): 1393-1398.
    • (2004) Nat Biotechnol , vol.22 , Issue.11 , pp. 1393-1398
    • Wurm, F.M.1
  • 18
    • 55849083888 scopus 로고    scopus 로고
    • DSC for studying carbohydrate effect on antibodies
    • Wen J, Jiang Y, Narhi L. 2008. DSC for studying carbohydrate effect on antibodies. Am Pharm Rev 11 (6): 98-104.
    • (2008) Am Pharm Rev , vol.11 , Issue.6 , pp. 98-104
    • Wen, J.1    Jiang, Y.2    Narhi, L.3
  • 19
    • 67449119292 scopus 로고    scopus 로고
    • Effects of glycosylation on the stability of protein pharmaceuticals
    • Sol RJ, Greibenow K. 2009. Effects of glycosylation on the stability of protein pharmaceuticals. J Pharm Sci 98: 1223-1245.
    • (2009) J Pharm Sci , vol.98 , pp. 1223-1245
    • Sol, R.J.1    Greibenow, K.2
  • 21
    • 34249807636 scopus 로고    scopus 로고
    • Inhibin A and B in vitro bioactivities are modified by their degrees of glycosylation and affinities to betaglycan
    • Makanji Y, Harrison CA, Stanton PG, Krishna R, Robertson DM. 2007. Inhibin A and B in vitro bioactivities are modified by their degrees of glycosylation and affinities to betaglycan. Endocrinology 148 (5): 2309-2316.
    • (2007) Endocrinology , vol.148 , Issue.5 , pp. 2309-2316
    • Makanji, Y.1    Harrison, C.A.2    Stanton, P.G.3    Krishna, R.4    Robertson, D.M.5
  • 22
    • 84886048718 scopus 로고    scopus 로고
    • Not all aggregates are the same: So should they all be removed
    • Presented at the American Chemical Society National Meeting Philadelphia PA August
    • Shultz JE, Jiang Y, Wen J, Li C, Ramachander R, Stenson R, Pampel L, Gokarn Y, Narhi LO. 2008. Not all aggregates are the same: So, should they all be removed? Presented at the American Chemical Society National Meeting, Philadelphia, PA, August.
    • (2008)
    • Shultz, J.E.1    Jiang, Y.2    Wen, J.3    Li, C.4    Ramachander, R.5    Stenson, R.6    Pampel, L.7    Gokarn, Y.8    Narhi, L.O.9
  • 23
    • 35748954020 scopus 로고    scopus 로고
    • Chaperone-assisted refolding of Escherichia coli maltodextrin glycosidase
    • Paul S, Punam S, Chaudhuri TK. 2007. Chaperone-assisted refolding of Escherichia coli maltodextrin glycosidase. FEBS J 274 (22): 6000-6010.
    • (2007) FEBS J , vol.274 , Issue.22 , pp. 6000-6010
    • Paul, S.1    Punam, S.2    Chaudhuri, T.K.3
  • 24
    • 33749057744 scopus 로고    scopus 로고
    • Protein aggregation and bioprocessing
    • Cromwell ME, Hilario E, Jacobson F. 2006. Protein aggregation and bioprocessing. AAPS J 8 (3): E572-579.
    • (2006) AAPS J , vol.8 , Issue.3 , pp. 572-579
    • Cromwell, M.E.1    Hilario, E.2    Jacobson, F.3
  • 25
    • 0037140419 scopus 로고    scopus 로고
    • Induction of protein aggregation in an early secretory compartment by elevation of expression level
    • Schroder M, Schafer R, Friedl P. 2002. Induction of protein aggregation in an early secretory compartment by elevation of expression level. Biotechnol Bioeng 78 (2): 131-140.
    • (2002) Biotechnol Bioeng , vol.78 , Issue.2 , pp. 131-140
    • Schroder, M.1    Schafer, R.2    Friedl, P.3
  • 26
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti A, Zhang Y, Hendershot LM, Harding HP, Ron D. 2000. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat Cell Biol 2 (6): 326-332.
    • (2000) Nat Cell Biol , vol.2 , Issue.6 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 27
    • 54049142921 scopus 로고    scopus 로고
    • Stabilizing protein-folding conformations
    • Lee GW. 2008. Stabilizing protein-folding conformations. Gen Eng Biotechnol News 28 (5): 60-63.
    • (2008) Gen Eng Biotechnol News , vol.28 , Issue.5 , pp. 60-63
    • Lee, G.W.1
  • 28
    • 0025789619 scopus 로고
    • Regulation of endoplasmic reticulum stress proteins in COS cells transfected with immunoglobulin mu heavy chain cDNA
    • Lenny N, Green M. 1991. Regulation of endoplasmic reticulum stress proteins in COS cells transfected with immunoglobulin mu heavy chain cDNA. J Biol Chem 266 (30): 20532-20537.
    • (1991) J Biol Chem , vol.266 , Issue.30 , pp. 20532-20537
    • Lenny, N.1    Green, M.2
  • 29
    • 13544259722 scopus 로고    scopus 로고
    • On the optimal ratio of heavy to light chain genes for efficient recombinant antibody production by CHO cells
    • Schlatter S, Stansfield SH, Dinnis DM, Racher AJ, Birch JR, James DC. 2005. On the optimal ratio of heavy to light chain genes for efficient recombinant antibody production by CHO cells. Biotechnol Prog 21 (1): 122-133.
    • (2005) Biotechnol Prog , vol.21 , Issue.1 , pp. 122-133
    • Schlatter, S.1    Stansfield, S.H.2    Dinnis, D.M.3    Racher, A.J.4    Birch, J.R.5    James, D.C.6
  • 30
    • 0034896499 scopus 로고    scopus 로고
    • Unassembled Ig heavy chains do not cycle from BiP in vivo but require light chains to trigger their release
    • Vanhove M, Usherwood YK, Hendershot LM. 2001. Unassembled Ig heavy chains do not cycle from BiP in vivo but require light chains to trigger their release. Immunity 15 (1): 105-114.
    • (2001) Immunity , vol.15 , Issue.1 , pp. 105-114
    • Vanhove, M.1    Usherwood, Y.K.2    Hendershot, L.M.3
  • 31
    • 60549105996 scopus 로고    scopus 로고
    • A clone screening method using mRNA levels to determine specific productivity and product quality for monoclonal antibodies
    • Lee CJ, Seth G, Tsukuda J, Hamilton RW. 2009. A clone screening method using mRNA levels to determine specific productivity and product quality for monoclonal antibodies. Biotechnol Bioeng 102 (4): 1107-1118.
    • (2009) Biotechnol Bioeng , vol.102 , Issue.4 , pp. 1107-1118
    • Lee, C.J.1    Seth, G.2    Tsukuda, J.3    Hamilton, R.W.4
  • 32
    • 0032942957 scopus 로고    scopus 로고
    • Influence of osmolarity and pH increase to achieve a reduction of monoclonal antibodies aggregates in a production process
    • Franco R, Daniela G, Fabrizio M, Ilaria G, Detlev H. 1999. Influence of osmolarity and pH increase to achieve a reduction of monoclonal antibodies aggregates in a production process. Cytotechnology 29 (1): 11-25.
    • (1999) Cytotechnology , vol.29 , Issue.1 , pp. 11-25
    • Franco, R.1    Daniela, G.2    Fabrizio, M.3    Ilaria, G.4    Detlev, H.5
  • 33
    • 83655195345 scopus 로고    scopus 로고
    • Use of low temperature and/or low pH in cell culture
    • US Patent Application # US20080269132 Wyeth
    • Gomes JM, Hiller GW. 2008. Use of low temperature and/or low pH in cell culture. US Patent Application # US20080269132, Wyeth.
    • (2008)
    • Gomes, J.M.1    Hiller, G.W.2
  • 34
    • 0032902878 scopus 로고    scopus 로고
    • Coxsackievirus and adenovirus receptor amino-terminal immunoglobulin V-related domain binds adenovirus type 2 and fiber knob from adenovirus type 12
    • Freimuth P, Springer K, Berard C, Hainfeld J, Bewley M, Flanagan J. 1999. Coxsackievirus and adenovirus receptor amino-terminal immunoglobulin V-related domain binds adenovirus type 2 and fiber knob from adenovirus type 12. J Virol 73 (2): 1392-1398.
    • (1999) J Virol , vol.73 , Issue.2 , pp. 1392-1398
    • Freimuth, P.1    Springer, K.2    Berard, C.3    Hainfeld, J.4    Bewley, M.5    Flanagan, J.6
  • 35
    • 16344374566 scopus 로고    scopus 로고
    • Effect of copper sulfate on performance of a serum-free CHO cell culture process and the level of free thiol in the recombinant antibody expressed
    • Chaderjian WB, Chin ET, Harris RJ, Etcheverry TM. 2005. Effect of copper sulfate on performance of a serum-free CHO cell culture process and the level of free thiol in the recombinant antibody expressed. Biotechnol Prog 21 (2): 550-553.
    • (2005) Biotechnol Prog , vol.21 , Issue.2 , pp. 550-553
    • Chaderjian, W.B.1    Chin, E.T.2    Harris, R.J.3    Etcheverry, T.M.4
  • 36
    • 84886033361 scopus 로고    scopus 로고
    • Methods of protein production using anti-senescence compounds
    • US Patent Application # US20080274507 Wyeth
    • Gomes JM, Hiller GW, Luan Y-T, Wang W. 2008. Methods of protein production using anti-senescence compounds. US Patent Application # US20080274507, Wyeth.
    • (2008)
    • Gomes, J.M.1    Hiller, G.W.2    Luan, Y.-T.3    Wang, W.4
  • 38
    • 0037447846 scopus 로고    scopus 로고
    • Detection and prevention of protein aggregation before, during, and after purification
    • Bondos SE, Bicknell A. 2003. Detection and prevention of protein aggregation before, during, and after purification. Anal Biochem 316 (2): 223-231.
    • (2003) Anal Biochem , vol.316 , Issue.2 , pp. 223-231
    • Bondos, S.E.1    Bicknell, A.2
  • 39
    • 0035223114 scopus 로고    scopus 로고
    • Stabilization of protein structure
    • Murphy KP. 2001. Stabilization of protein structure. Methods Mol Biol 168: 1-16.
    • (2001) Methods Mol Biol , vol.168 , pp. 1-16
    • Murphy, K.P.1
  • 40
    • 0025843479 scopus 로고
    • A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme
    • Goldberg ME, Rudolph R, Jaenicke R. 1991. A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme. Biochemistry 30 (11): 2790-2797.
    • (1991) Biochemistry , vol.30 , Issue.11 , pp. 2790-2797
    • Goldberg, M.E.1    Rudolph, R.2    Jaenicke, R.3
  • 41
    • 0021690181 scopus 로고
    • Reversible self-association of a human myeloma protein Thermodynamics and relevance to viscosity effects and solubility
    • Hall CG, Abraham GN. 1984. Reversible self-association of a human myeloma protein. Thermodynamics and relevance to viscosity effects and solubility. Biochemistry 23 (22): 5123-5129.
    • (1984) Biochemistry , vol.23 , Issue.22 , pp. 5123-5129
    • Hall, C.G.1    Abraham, G.N.2
  • 42
    • 84885986269 scopus 로고    scopus 로고
    • Purification processes-Sorting out the good the bad and the ugly
    • Presented at the Recovery of Biological Products XIII Conference Philadelphia PA June
    • Mire-Sluis A. 2008. Purification processes-Sorting out the good, the bad and the ugly. Presented at the Recovery of Biological Products XIII Conference, Philadelphia, PA, June.
    • (2008)
    • Mire-Sluis, A.1
  • 43
    • 0020477017 scopus 로고
    • Stabilization of protein structure by sugars
    • Arakawa T, Timasheff SN. 1982. Stabilization of protein structure by sugars. Biochemistry 21 (25): 6536-6544.
    • (1982) Biochemistry , vol.21 , Issue.25 , pp. 6536-6544
    • Arakawa, T.1    Timasheff, S.N.2
  • 45
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability
    • Baldwin RL. 1996. How Hofmeister ion interactions affect protein stability. Biophys J 71 (4): 2056-2063.
    • (1996) Biophys J , vol.71 , Issue.4 , pp. 2056-2063
    • Baldwin, R.L.1
  • 46
    • 11944271430 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. Biotechnology 8 (4): 308-317.
    • (1990) Biotechnology , vol.8 , Issue.4 , pp. 308-317
    • Schein, C.H.1
  • 48
    • 0030043206 scopus 로고    scopus 로고
    • Proteins in frozen solutions-Evidence of ice-induced partial unfolding
    • Strambini GB, Gabellieri E. 1996. Proteins in frozen solutions-Evidence of ice-induced partial unfolding. Biophys J 70 (2): 971-976.
    • (1996) Biophys J , vol.70 , Issue.2 , pp. 971-976
    • Strambini, G.B.1    Gabellieri, E.2
  • 49
    • 0031660957 scopus 로고    scopus 로고
    • Effects of Tween 80 and sucrose on acute short-term stability and long-term storage at-20 degrees C of a recombinant hemoglobin
    • Kerwin BA, Heller M, Levin SH, Randolph TW. 1998. Effects of Tween 80 and sucrose on acute short-term stability and long-term storage at-20 degrees C of a recombinant hemoglobin. J Pharm Sci 87 (9): 1062-1068.
    • (1998) J Pharm Sci , vol.87 , Issue.9 , pp. 1062-1068
    • Kerwin, B.A.1    Heller, M.2    Levin, S.H.3    Randolph, T.W.4
  • 50
    • 0028286684 scopus 로고
    • Molecular cloning and functions of rat liver hydroxysteroid sulfotransferases catalysing covalent binding of carcinogenic polycyclic arylmethanols to DNA
    • Watabe T, Ogura K, Satsukawa M, Okuda H, Hiratsuka A. 1994. Molecular cloning and functions of rat liver hydroxysteroid sulfotransferases catalysing covalent binding of carcinogenic polycyclic arylmethanols to DNA. Chem Biol Interact 92 (1-3): 87-105.
    • (1994) Chem Biol Interact , vol.92 , Issue.1-3 , pp. 87-105
    • Watabe, T.1    Ogura, K.2    Satsukawa, M.3    Okuda, H.4    Hiratsuka, A.5
  • 51
    • 0027264639 scopus 로고
    • Thermal stability of low molecular weight urokinase during heat treatment I. Effects of protein concentration, pH and ionic strength
    • Porter WR, Staack H, Brandt K, Manning MC. 1993. Thermal stability of low molecular weight urokinase during heat treatment. I. Effects of protein concentration, pH and ionic strength. Thromb Res 71 (4): 265-279.
    • (1993) Thromb Res , vol.71 , Issue.4 , pp. 265-279
    • Porter, W.R.1    Staack, H.2    Brandt, K.3    Manning, M.C.4
  • 53
    • 84886042740 scopus 로고    scopus 로고
    • Post-refolding harvest of E. coli expressed Fc-fusion proteins
    • Presented at the BioProcess International World Conference Boston September
    • Hart RA, Smith SG, Shultz JE. 2005. Post-refolding harvest of E. coli expressed Fc-fusion proteins. Presented at the BioProcess International World Conference, Boston, September.
    • (2005)
    • Hart, R.A.1    Smith, S.G.2    Shultz, J.E.3
  • 54
    • 41049112488 scopus 로고    scopus 로고
    • Modeling of protein monomer/aggregate purification and separation using hydrophobic interaction chromatography
    • McCue JT, Engel P, Ng A, Macniven R, Thommes J. 2008. Modeling of protein monomer/aggregate purification and separation using hydrophobic interaction chromatography. Bioprocess Biosyst Eng 31 (3): 261-275.
    • (2008) Bioprocess Biosyst Eng , vol.31 , Issue.3 , pp. 261-275
    • McCue, J.T.1    Engel, P.2    Ng, A.3    Macniven, R.4    Thommes, J.5
  • 55
    • 84885965417 scopus 로고    scopus 로고
    • Improving upstream feed stock to downstream operations
    • Presented at the Recovery of Biological Products XIII Quebec City Quebec Canada June
    • Yigsaw Y. 2008. Improving upstream feed stock to downstream operations. Presented at the Recovery of Biological Products XIII, Quebec City, Quebec, Canada, June 22-27.
    • (2008) , pp. 22-27
    • Yigsaw, Y.1
  • 56
    • 0032855077 scopus 로고    scopus 로고
    • Inhibition of aggregation side reactions during in vitro protein folding
    • Clark EDB, Schwarz E, Rudolph R. 1999. Inhibition of aggregation side reactions during in vitro protein folding. Methods Enzymol 309: 217-236.
    • (1999) Methods Enzymol , vol.309 , pp. 217-236
    • Clark, E.D.B.1    Schwarz, E.2    Rudolph, R.3
  • 57
    • 0031950560 scopus 로고    scopus 로고
    • Refolding of recombinant proteins
    • Clark EDB. 1998. Refolding of recombinant proteins. Curr Opin Biotechnol 9: 157-163.
    • (1998) Curr Opin Biotechnol , vol.9 , pp. 157-163
    • Clark, E.D.B.1
  • 58
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • Fink AL. 1998. Protein aggregation: Folding aggregates, inclusion bodies and amyloid. Fold Des 3: R9-R23.
    • (1998) Fold Des , vol.3 , pp. 9-23
    • Fink, A.L.1
  • 59
    • 0035861633 scopus 로고    scopus 로고
    • High pressure refolding of recombinant human growth hormone from insoluble aggregates Structural transformations, kinetic barriers, and energetics
    • St John RJ, Carpenter JF, Balny C, Randolph TW. 2001. High pressure refolding of recombinant human growth hormone from insoluble aggregates. Structural transformations, kinetic barriers, and energetics. J Biol Chem 276 (50): 46856-46863.
    • (2001) J Biol Chem , vol.276 , Issue.50 , pp. 46856-46863
    • St John, R.J.1    Carpenter, J.F.2    Balny, C.3    Randolph, T.W.4
  • 60
    • 0034647650 scopus 로고    scopus 로고
    • High-pressure denaturation of apomyoglobin
    • Bondos SE, Sligar S, Jonas J. 2000. High-pressure denaturation of apomyoglobin. Biochim Biophys Acta 1480 (1-2): 353-364.
    • (2000) Biochim Biophys Acta , vol.1480 , Issue.1-2 , pp. 353-364
    • Bondos, S.E.1    Sligar, S.2    Jonas, J.3
  • 61
    • 58149216346 scopus 로고    scopus 로고
    • IgG particle formation during filling pump operation: A case study of heterogeneous nucleation on stainless steel nanoparticles
    • Tyagi AK, Randolph TW, Dong A, Maloney KM, Hitscherich C Jr., Carpenter JF. 2009. IgG particle formation during filling pump operation: A case study of heterogeneous nucleation on stainless steel nanoparticles. J Pharm Sci 98: 94-104.
    • (2009) J Pharm Sci , vol.98 , pp. 94-104
    • Tyagi, A.K.1    Randolph, T.W.2    Dong, A.3    Maloney, K.M.4    Hitscherich Jr., C.5    Carpenter, J.F.6
  • 62
    • 0035811224 scopus 로고    scopus 로고
    • Scale-down model to simulate spatial pH variations in large-scale bioreactors
    • Amanullah A, McFarlane CM, Emery AN, Nienow AW. 2001. Scale-down model to simulate spatial pH variations in large-scale bioreactors. Biotechnol Bioeng 73 (5): 390-399.
    • (2001) Biotechnol Bioeng , vol.73 , Issue.5 , pp. 390-399
    • Amanullah, A.1    McFarlane, C.M.2    Emery, A.N.3    Nienow, A.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.