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Volumn 117, Issue 30, 2013, Pages 8939-8946

Measuring and modeling hemoglobin aggregation below the freezing temperature

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATION KINETICS; AGGREGATION MECHANISM; FREEZING TEMPERATURES; INITIAL CONCENTRATION; PROTEIN AGGREGATION; SOLUTE CONCENTRATIONS; STORAGE TEMPERATURES; THERMODYNAMIC INFORMATION;

EID: 84881244021     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp4035369     Document Type: Article
Times cited : (29)

References (38)
  • 1
    • 79955581681 scopus 로고    scopus 로고
    • Fundamental Structures and Behaviors of Proteins
    • Wang, W. Roberts, C. John Wiley & Sons, Inc. Hoboken, NJ
    • Laurence, J. S.; Middaugh, C. R. Fundamental Structures and Behaviors of Proteins. In Aggregation of Therapeutic Proteins; Wang, W., Roberts, C., Eds.; John Wiley & Sons, Inc.: Hoboken, NJ, 2010; pp 1-62.
    • (2010) Aggregation of Therapeutic Proteins , pp. 1-62
    • Laurence, J.S.1    Middaugh, C.R.2
  • 2
    • 78650543555 scopus 로고    scopus 로고
    • Impact of Product-Related Factors on Immunogenicity of Biotherapeutics
    • Singh, S. K. Impact of Product-Related Factors on Immunogenicity of Biotherapeutics J. Pharm. Sci. 2011, 100, 354-387
    • (2011) J. Pharm. Sci. , vol.100 , pp. 354-387
    • Singh, S.K.1
  • 3
    • 33748041958 scopus 로고    scopus 로고
    • Effects of Protein Aggregates: An Immunologic Perspective
    • Rosenberg, A. S. Effects of Protein Aggregates: An Immunologic Perspective AAPS J. 2006, 8, E501-E507
    • (2006) AAPS J. , vol.8
    • Rosenberg, A.S.1
  • 4
    • 79955599896 scopus 로고    scopus 로고
    • Frozen State Storage Instability of a Monoclonal Antibody: Aggregation as a Consequence of Trehalose Crystallization and Protein Unfolding
    • Singh, S. K.; Kolhe, P.; Mehta, A. P.; Chico, S. C.; Lary, A. L.; Huang, M. Frozen State Storage Instability of a Monoclonal Antibody: Aggregation as a Consequence of Trehalose Crystallization and Protein Unfolding Pharm. Res. 2011, 28, 873-885
    • (2011) Pharm. Res. , vol.28 , pp. 873-885
    • Singh, S.K.1    Kolhe, P.2    Mehta, A.P.3    Chico, S.C.4    Lary, A.L.5    Huang, M.6
  • 5
    • 0036250675 scopus 로고    scopus 로고
    • Freezing Biopharmaceuticals Using Common Techniques - And the Magnitude of Bulk-Scale Freeze-Concentration
    • Webb, S. D.; Sesin, D. F.; Kincaid, A. C.; Webb, J. N.; Hughes, T. G. Freezing Biopharmaceuticals Using Common Techniques-And the Magnitude of Bulk-Scale Freeze-Concentration BioPharm Int. 2002, 15, 22-34
    • (2002) BioPharm Int. , vol.15 , pp. 22-34
    • Webb, S.D.1    Sesin, D.F.2    Kincaid, A.C.3    Webb, J.N.4    Hughes, T.G.5
  • 6
    • 67651202371 scopus 로고    scopus 로고
    • Freezing-Induced Phase Separation and Spatial Microheterogeneity in Protein Solutions
    • Dong, J.; Hubel, A.; Bischof, J. C.; Aksan, A. Freezing-Induced Phase Separation and Spatial Microheterogeneity in Protein Solutions J. Phys. Chem. B 2009, 113, 10081-10087
    • (2009) J. Phys. Chem. B , vol.113 , pp. 10081-10087
    • Dong, J.1    Hubel, A.2    Bischof, J.C.3    Aksan, A.4
  • 7
    • 77953674463 scopus 로고    scopus 로고
    • Cold Denaturation of Monoclonal Antibodies
    • Lazar, K. L.; Patapoff, T. W.; Sharma, V. K. Cold Denaturation of Monoclonal Antibodies mAbs 2010, 2, 42-52
    • (2010) MAbs , vol.2 , pp. 42-52
    • Lazar, K.L.1    Patapoff, T.W.2    Sharma, V.K.3
  • 8
    • 35748979712 scopus 로고    scopus 로고
    • Protein Stability during Freezing: Separation of Stresses and Mechanisms of Protein Stabilization
    • Bhatnagar, B. S.; Bogner, R. H.; Pikal, M. J. Protein Stability During Freezing: Separation of Stresses and Mechanisms of Protein Stabilization Pharm. Dev. Technol. 2007, 12, 505-523
    • (2007) Pharm. Dev. Technol. , vol.12 , pp. 505-523
    • Bhatnagar, B.S.1    Bogner, R.H.2    Pikal, M.J.3
  • 9
    • 0036771258 scopus 로고    scopus 로고
    • Effect of Glycine on pH Changes and Protein Stability during Freeze-Thawing in Phosphate Buffer systems
    • Pikal-Cleland, K. A.; Cleland, J. L.; Anchordoquy, T. J.; Carpenter, J. F. Effect of Glycine on pH Changes and Protein Stability during Freeze-Thawing in Phosphate Buffer systems J. Pharm. Sci. 2002, 91, 1969-1979
    • (2002) J. Pharm. Sci. , vol.91 , pp. 1969-1979
    • Pikal-Cleland, K.A.1    Cleland, J.L.2    Anchordoquy, T.J.3    Carpenter, J.F.4
  • 10
    • 23844447975 scopus 로고    scopus 로고
    • Mechanism of Protein Stabilization by Sugars during Freeze-Drying and Storage: Native Structure Preservation, Specific Interaction, and/or Immobilization in a Glassy Matrix?
    • Chang, L. L.; Shepherd, D.; Sun, J.; Ouellette, D.; Grant, K. L.; Tang, X. C.; Pikal, M. J. Mechanism of Protein Stabilization by Sugars during Freeze-Drying and Storage: Native Structure Preservation, Specific Interaction, and/or Immobilization in a Glassy Matrix? J. Pharm. Sci. 2005, 94, 1427-1444
    • (2005) J. Pharm. Sci. , vol.94 , pp. 1427-1444
    • Chang, L.L.1    Shepherd, D.2    Sun, J.3    Ouellette, D.4    Grant, K.L.5    Tang, X.C.6    Pikal, M.J.7
  • 12
    • 0036367093 scopus 로고    scopus 로고
    • Physical Stabilization of Proteins in Aqueous Solution
    • Carpenter, J. F. Manning, M. C. Kluwer Academic/Plenum Publishers: New York
    • Kendrick, B. S.; Li, T.; Chang, B. S. Physical Stabilization of Proteins in Aqueous Solution. In Rationale Design of Stable Protein Formulations-Theory and Practice; Carpenter, J. F.; Manning, M. C., Eds.; Kluwer Academic/Plenum Publishers: New York, 2002; Vol. 13, pp 61-84.
    • (2002) Rationale Design of Stable Protein Formulations - Theory and Practice , vol.13 , pp. 61-84
    • Kendrick, B.S.1    Li, T.2    Chang, B.S.3
  • 13
    • 0029198906 scopus 로고
    • Solvent Stabilization of Protein Structure
    • Timasheff, S. N. Solvent Stabilization of Protein Structure Methods Mol. Biol. (N. Y., NY) 1995, 40, 253-269
    • (1995) Methods Mol. Biol. (N. Y., NY) , vol.40 , pp. 253-269
    • Timasheff, S.N.1
  • 15
    • 33751249357 scopus 로고    scopus 로고
    • Cryoglobulins: An Important but Neglected Clinical Test
    • Shihabi, Z. K. Cryoglobulins: An Important but Neglected Clinical Test Ann. Clin. Lab. Sci. 2006, 36, 395-408
    • (2006) Ann. Clin. Lab. Sci. , vol.36 , pp. 395-408
    • Shihabi, Z.K.1
  • 17
    • 50849128798 scopus 로고    scopus 로고
    • Viscosity of Concentrated Sucrose and Trehalose Aqueous Solutions Including the Supercooled Regime
    • Longinotti, M. P.; Corti, H. R. Viscosity of Concentrated Sucrose and Trehalose Aqueous Solutions Including the Supercooled Regime J. Phys. Chem. Ref. Data 2008, 37, 1503-1515
    • (2008) J. Phys. Chem. Ref. Data , vol.37 , pp. 1503-1515
    • Longinotti, M.P.1    Corti, H.R.2
  • 18
    • 0002862399 scopus 로고
    • Denaturation of Hemoglobin under High Pressure i
    • Suzuki, K.; Kitamura, K. Denaturation of Hemoglobin under High Pressure I Rev. Phys. Chem. Jpn. 1960, 29, 81-85
    • (1960) Rev. Phys. Chem. Jpn. , vol.29 , pp. 81-85
    • Suzuki, K.1    Kitamura, K.2
  • 19
    • 0028220701 scopus 로고
    • Proteins under Pressure - The Influence of High Hydrostatic Pressure on Structure, Function and Assembly of Proteins and Protein Complexes
    • Gross, M.; Jaenicke, R. Proteins under Pressure-The Influence of High Hydrostatic Pressure on Structure, Function and Assembly of Proteins and Protein Complexes Eur. J. Biochem. 1994, 221, 617-630
    • (1994) Eur. J. Biochem. , vol.221 , pp. 617-630
    • Gross, M.1    Jaenicke, R.2
  • 20
    • 0012223420 scopus 로고    scopus 로고
    • High Pressure and Protein Oligomeric Dissociation
    • Balny, C. High Pressure and Protein Oligomeric Dissociation High Pressure Res. 2002, 22, 737-741
    • (2002) High Pressure Res. , vol.22 , pp. 737-741
    • Balny, C.1
  • 21
    • 24344491042 scopus 로고    scopus 로고
    • High-Pressure Studies of Aggregation of Recombinant Human Interleukin-1 Receptor Antagonist: Thermodynamics, Kinetics, and Application to Accelerated Formulation Studies
    • Seefeldt, M. B.; Kim, Y. S.; Tolley, K. P.; Seely, J.; Carpenter, J. F.; Randolph, T. W. High-Pressure Studies of Aggregation of Recombinant Human Interleukin-1 Receptor Antagonist: Thermodynamics, Kinetics, and Application to Accelerated Formulation Studies Protein Sci. 2005, 14, 2258-2266
    • (2005) Protein Sci. , vol.14 , pp. 2258-2266
    • Seefeldt, M.B.1    Kim, Y.S.2    Tolley, K.P.3    Seely, J.4    Carpenter, J.F.5    Randolph, T.W.6
  • 22
    • 0008823209 scopus 로고    scopus 로고
    • Pressure-Assisted Cold Unfolding of Proteins and Its Effects on the Conformational Stability Compared to Pressure and Heat Unfolding
    • Meersman, F.; Smeller, L.; Heremans, K. Pressure-Assisted Cold Unfolding of Proteins and Its Effects on the Conformational Stability Compared to Pressure and Heat Unfolding High Pressure Res. 2000, 19, 263-268
    • (2000) High Pressure Res. , vol.19 , pp. 263-268
    • Meersman, F.1    Smeller, L.2    Heremans, K.3
  • 23
    • 59349083966 scopus 로고    scopus 로고
    • Protein Aggregation Kinetics, Mechanism, and Curve-Fitting: A Review of the Literature
    • Morris, A. M.; Watzky, M. A.; Finke, R. G. Protein Aggregation Kinetics, Mechanism, and Curve-Fitting: A Review of the Literature Biochim. Biophys. Acta 2009, 1794, 375-397
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 375-397
    • Morris, A.M.1    Watzky, M.A.2    Finke, R.G.3
  • 25
    • 0036070790 scopus 로고    scopus 로고
    • Thermal Denaturation of Bungarus fasciatus Acetylcholinesterase: Is Aggregation a Driving Force in Protein Unfolding?
    • Shin, I.; Wachtel, E.; Roth, E.; Bon, C.; Silman, I.; Weiner, L. Thermal Denaturation of Bungarus fasciatus Acetylcholinesterase: Is Aggregation a Driving Force in Protein Unfolding? Protein Sci. 2002, 11, 2022-2032
    • (2002) Protein Sci. , vol.11 , pp. 2022-2032
    • Shin, I.1    Wachtel, E.2    Roth, E.3    Bon, C.4    Silman, I.5    Weiner, L.6
  • 26
    • 0037421836 scopus 로고    scopus 로고
    • Kinetics of Irreversible Protein Aggregation: Analysis of Extended Lumry-Eyring Models and Implications for Predicting Protein Shelf Life
    • Roberts, C. J. Kinetics of Irreversible Protein Aggregation: Analysis of Extended Lumry-Eyring Models and Implications for Predicting Protein Shelf Life J. Phys. Chem. B 2003, 107, 1194-1207
    • (2003) J. Phys. Chem. B , vol.107 , pp. 1194-1207
    • Roberts, C.J.1
  • 27
    • 67650072650 scopus 로고    scopus 로고
    • Lumry-Eyring Nucleated-Polymerization Model of Protein Aggregation Kinetics: 2. Competing Growth via Condensation and Chain Polymerization
    • Li, Y.; Roberts, C. J. Lumry-Eyring Nucleated-Polymerization Model of Protein Aggregation Kinetics: 2. Competing Growth via Condensation and Chain Polymerization J. Phys. Chem. B 2009, 113, 7020-7032
    • (2009) J. Phys. Chem. B , vol.113 , pp. 7020-7032
    • Li, Y.1    Roberts, C.J.2
  • 28
    • 34250834054 scopus 로고    scopus 로고
    • A Lumry-Eyring Nucleated Polymerization Model of Protein Aggregation Kinetics: 1. Aggregation with Pre-Equilibrated Unfolding
    • Andrews, J. M.; Roberts, C. J. A Lumry-Eyring Nucleated Polymerization Model of Protein Aggregation Kinetics: 1. Aggregation with Pre-Equilibrated Unfolding J. Phys. Chem. B 2007, 11, 7897-7913
    • (2007) J. Phys. Chem. B , vol.11 , pp. 7897-7913
    • Andrews, J.M.1    Roberts, C.J.2
  • 29
    • 64549100352 scopus 로고    scopus 로고
    • Tangential Flow Filtration of Hemoglobin
    • Palmer, A. F.; Sun, G.; Harris, D. R. Tangential Flow Filtration of Hemoglobin Biotechnol. Prog. 2009, 25, 189-199
    • (2009) Biotechnol. Prog. , vol.25 , pp. 189-199
    • Palmer, A.F.1    Sun, G.2    Harris, D.R.3
  • 30
    • 0029937808 scopus 로고    scopus 로고
    • Recommendations for Reference Method for Haemoglobinometry in Human Blood (ICSH Standard 1995) and Specifications for International Haemiglobinocyanide Standard (4th Edition)
    • Zwart, A.; van Assendelft, O. W.; Bull, B. S.; England, J. M.; Lewis, S. M.; Zijlstra, W. G. Recommendations for Reference Method for Haemoglobinometry in Human Blood (ICSH Standard 1995) and Specifications for International Haemiglobinocyanide Standard (4th Edition) J. Clin. Pathol. 1996, 49, 271-274
    • (1996) J. Clin. Pathol. , vol.49 , pp. 271-274
    • Zwart, A.1    Van Assendelft, O.W.2    Bull, B.S.3    England, J.M.4    Lewis, S.M.5    Zijlstra, W.G.6
  • 31
    • 0001962269 scopus 로고
    • Principle of "cryostabilization" Technology from Structure/Property Relationships of Carbohydrate/Water Systems-A Review
    • Levine, H.; Slade, L. Principle of "Cryostabilization" Technology from Structure/Property Relationships of Carbohydrate/Water Systems-A Review CryoLetters 1988, 9, 21-63
    • (1988) CryoLetters , vol.9 , pp. 21-63
    • Levine, H.1    Slade, L.2
  • 32
    • 0842302347 scopus 로고    scopus 로고
    • Trehalose-Enzyme Interactions Result in Structure Stabilization and Activity Inhibition. The Role of Viscosity
    • Sampedro, J. G.; Uribe, S. Trehalose-Enzyme Interactions Result in Structure Stabilization and Activity Inhibition. The Role of Viscosity Mol. Cell. Biochem. 2004, 256, 319-327
    • (2004) Mol. Cell. Biochem. , vol.256 , pp. 319-327
    • Sampedro, J.G.1    Uribe, S.2
  • 33
    • 0023905575 scopus 로고
    • The Mechanism of Cryoprotection of Proteins by Solutes
    • Carpenter, J. F.; Crowe, J. H. The Mechanism of Cryoprotection of Proteins by Solutes Cryobiology 1988, 25, 244-255
    • (1988) Cryobiology , vol.25 , pp. 244-255
    • Carpenter, J.F.1    Crowe, J.H.2
  • 34
    • 0019888281 scopus 로고
    • The Stabilization of Proteins by Sucrose
    • Lee, J. C.; Thimaseff, S. N. The Stabilization of Proteins by Sucrose J. Biol. Chem. 1981, 256, 7193-7201
    • (1981) J. Biol. Chem. , vol.256 , pp. 7193-7201
    • Lee, J.C.1    Thimaseff, S.N.2
  • 36
    • 84874723211 scopus 로고    scopus 로고
    • Frozen-State Storage Stability of a Monoclonal Antibody: Aggregation is Impacted by Freezing Rate and Solute Distribution
    • Miller, M. A.; Rodrigues, M. A.; Glass, M. A.; Singh, S. K.; Johnston, K. P.; Maynard, J. A. Frozen-State Storage Stability of a Monoclonal Antibody: Aggregation is Impacted by Freezing Rate and Solute Distribution J. Pharm. Sci. 2013, 102, 1194-1208
    • (2013) J. Pharm. Sci. , vol.102 , pp. 1194-1208
    • Miller, M.A.1    Rodrigues, M.A.2    Glass, M.A.3    Singh, S.K.4    Johnston, K.P.5    Maynard, J.A.6
  • 37
    • 56449087972 scopus 로고    scopus 로고
    • The Hyperthermophilic Nature of the Metallo-Oxidase from Aquifex aeolicus
    • Fernandes, A. T.; Martins, L. O.; Melo, E. P. The Hyperthermophilic Nature of the Metallo-Oxidase from Aquifex aeolicus Biochim. Biophys. Acta 2009, 1794, 75-83
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 75-83
    • Fernandes, A.T.1    Martins, L.O.2    Melo, E.P.3
  • 38
    • 0034694819 scopus 로고    scopus 로고
    • Trehalose Delays the Reversible but Not the Irreversible Thermal Denaturation of Cutinase
    • Baptista, R. P.; Cabral, J. M.; Melo, E. P. Trehalose Delays the Reversible but Not the Irreversible Thermal Denaturation of Cutinase Biotechnol. Bioeng. 2000, 70, 699-703
    • (2000) Biotechnol. Bioeng. , vol.70 , pp. 699-703
    • Baptista, R.P.1    Cabral, J.M.2    Melo, E.P.3


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