메뉴 건너뛰기




Volumn 98, Issue 9, 2009, Pages 2954-2969

Mixing properties of lyophilized protein systems: A spectroscopic and calorimetric study

Author keywords

Calorimetry (DSC); Freeze drying lyophilization; Mixing; Protein formulation; Proteins; Spectroscopy; Thermal analysis; Thermodynamics

Indexed keywords

HETASTARCH; RIBONUCLEASE A; SUCROSE; TREHALOSE; UNCLASSIFIED DRUG; VIASTARCH;

EID: 68949122435     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.21467     Document Type: Article
Times cited : (27)

References (65)
  • 1
    • 0029815193 scopus 로고    scopus 로고
    • Counteracting effects of thiocyanate and sucrose on chymotrypsinogen secondary structure and aggregation during freezing, drying, and rehydration
    • Allison SD, Dong A, Carpenter JF. 1996. Counteracting effects of thiocyanate and sucrose on chymotrypsinogen secondary structure and aggregation during freezing, drying, and rehydration. Biophys J 71:2022-2032. (Pubitemid 26325980)
    • (1996) Biophysical Journal , vol.71 , Issue.4 , pp. 2022-2032
    • Allison, S.D.1    Dong, A.2    Carpenter, J.F.3
  • 2
    • 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. Biophys J 65:661-671. (Pubitemid 23263878)
    • (1993) Biophysical Journal , vol.65 , Issue.2 , pp. 661-671
    • Prestrelski, S.J.1    Tedeschi, N.2    Arakawa, T.3    Carpenter, J.F.4
  • 3
    • 0033562141 scopus 로고    scopus 로고
    • Hydrogen bonding between sugar and protein is responsible for inhibition of dehydration-induced protein unfolding
    • DOI 10.1006/abbi.1999.1175
    • Allison SD, Chang B, Randolph TW, Carpenter JF. 1999. Hydrogen bonding between sugar and protein is responsible for inhibition of dehydration-induced protein unfolding. Arch Biochem Biophys 365:289-298. (Pubitemid 29391638)
    • (1999) Archives of Biochemistry and Biophysics , vol.365 , Issue.2 , pp. 289-298
    • Allison, S.D.1    Chang, B.2    Randolph, T.W.3    Carpenter, J.F.4
  • 4
    • 0024549238 scopus 로고
    • An infrared spectroscopic study of the interaction of carbohydrates with dried proteins
    • Carpenter JF, Crowe JH. 1989. An infrared spectroscopic study of the interaction of carbohydrates with dried proteins. Biochemistry 28:3916-3922.
    • (1989) Biochemistry , vol.28 , pp. 3916-3922
    • Carpenter, J.F.1    Crowe, J.H.2
  • 6
    • 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:E10.
    • (2003) AAPS PharmSci , vol.5
    • Andya, J.D.1    Hsu, C.C.2    Shire, S.J.3
  • 7
    • 0031797174 scopus 로고    scopus 로고
    • Sugar-polymer hydrogen bond interactions in lyophilized amorphous mixtures
    • Taylor LS, Zografi G. 1998. Sugar-polymer hydrogen bond interactions in lyophilized amorphous mixtures. J Pharm Sci 87:1615-1621.
    • (1998) J Pharm Sci , vol.87 , pp. 1615-1621
    • Taylor, L.S.1    Zografi, G.2
  • 9
    • 0001665731 scopus 로고
    • Thermodynamics of polymer compatibility
    • Patterson D, Robard A. 1978. Thermodynamics of polymer compatibility. Macromolecules 11:690-695.
    • (1978) Macromolecules , vol.11 , pp. 690-695
    • Patterson, D.1    Robard, A.2
  • 10
    • 0026221658 scopus 로고
    • Effect of hydrogen-bonding on the enthalpy of mixing and the composition dependence of the glass-transition temperature in polymer blends
    • Painter PC, Graf JF, Coleman MM. 1991. Effect of hydrogen-bonding on the enthalpy of mixing and the composition dependence of the glass-transition temperature in polymer blends. Macromolecules 24:5630-5638.
    • (1991) Macromolecules , vol.24 , pp. 5630-5638
    • Painter, P.C.1    Graf, J.F.2    Coleman, M.M.3
  • 11
    • 0029250969 scopus 로고
    • Thermodynamic study of glass transitions in miscible polymer blends
    • Chee KK. 1995. Thermodynamic study of glass transitions in miscible polymer blends. Polymer 36:809-813.
    • (1995) Polymer , vol.36 , pp. 809-813
    • Chee, K.K.1
  • 12
    • 0345669819 scopus 로고
    • The effect of hydrogen bonding on the glass transition temperature of polymer mixtures
    • Kwei TK. 1984. The effect of hydrogen bonding on the glass transition temperature of polymer mixtures. J Polym Sci Polym Lett Ed 22:307-313.
    • (1984) J Polym Sci Polym Lett Ed , vol.22 , pp. 307-313
    • Kwei, T.K.1
  • 13
    • 1642462820 scopus 로고    scopus 로고
    • Miscibility and specific interactions in blends of poly(vinyl phenyl ketone hydrogenated) with poly(2,6-dimethyl-1,4-phenylene oxide)
    • DOI 10.1002/app.13242
    • Maldonado-Santoyo M, Ortiz-Estrada C, Luna-Barcenas G, Sanchez IC, Cesteros LC, Katime I, Nuno-Donlucas SM. 2004. Miscibility behavior and hydrogen bonding in blends of poly(vinyl phenyl ketone hydrogenated) and poly(2-ethyl-2-oxazoline). J Polym Sci Part B Polym Phys 42:636-645. (Pubitemid 38107438)
    • (2004) Journal of Applied Polymer Science , vol.91 , Issue.3 , pp. 1887-1892
    • Maldonado-Santoyo, M.1    Nuno-Donlucas, S.M.2    Cesteros, L.C.3    Katime, I.4
  • 14
    • 20444407280 scopus 로고    scopus 로고
    • An unusual, completely miscible, ternary hydrogen-bonded polymer blend of phenoxy, phenolic, and PCL
    • Kuo SW, Chan SC, Wu HD, Chang FC. 2005. An unusual, completely miscible, ternary hydrogen-bonded polymer blend of phenoxy, phenolic, and PCL. Macromolecules 38:4729-4736.
    • (2005) Macromolecules , vol.38 , pp. 4729-4736
    • Kuo, S.W.1    Chan, S.C.2    Wu, H.D.3    Chang, F.C.4
  • 15
    • 0033637883 scopus 로고    scopus 로고
    • Freeze-concentration separates protein and polymer. Excipients into different amorphous phases
    • Izutsu K, Kojima S. 2000a. Freeze-concentration separates protein and polymer. Excipients into different amorphous phases. Pharm Res 17:1316-1322.
    • (2000) Pharm Res , vol.17 , pp. 1316-1322
    • Izutsu, K.1    Kojima, S.2
  • 16
    • 0030712895 scopus 로고    scopus 로고
    • Phase separation of excipients during lyophilization: Effects on protein stability
    • Randolph TW. 1997. Phase separation of excipients during lyophilization: Effects on protein stability. J Pharm Sci 86:1198-1203.
    • (1997) J Pharm Sci , vol.86 , pp. 1198-1203
    • Randolph, T.W.1
  • 17
    • 0034933284 scopus 로고    scopus 로고
    • The ice nucleation temperature determines the primary drying rate of lyophilization for samples frozen on a temperature-controlled shelf
    • Searles JA, Carpenter JF, Randolph TW. 2001. The ice nucleation temperature determines the primary drying rate of lyophilization for samples frozen on a temperature-controlled shelf. J Pharm Sci 90:860-871.
    • (2001) J Pharm Sci , vol.90 , pp. 860-871
    • Searles, J.A.1    Carpenter, J.F.2    Randolph, T.W.3
  • 18
    • 21644451625 scopus 로고    scopus 로고
    • Effect of pH, counter ion, and phosphate concentration on the glass transition temperature of freeze-dried sugar-phosphate mixtures
    • DOI 10.1023/B:PHAM.0000041456.19377.87
    • Ohtake S, Schebor C, Palecek SP, de Pablo JJ. 2004. Effect of pH, counter ion, and phosphate concentration on the glass transition temperature of freeze-dried sugar-phosphate mixtures. Pharm Res 21:1615-1621. (Pubitemid 41184392)
    • (2004) Pharmaceutical Research , vol.21 , Issue.9 , pp. 1615-1621
    • Ohtake, S.1    Schebor, C.2    Palecek, S.P.3    De Pablo, J.J.4
  • 19
    • 0344012508 scopus 로고    scopus 로고
    • Understanding the Physical Stability of Freeze Dried Dosage Forms from the Glass Transition Temperature of the Amorphous Components
    • DOI 10.1002/jps.10474
    • Fitzpatrick S, Saklatvala R. 2003. Understanding the physical stability of freeze dried dosage forms from the glass transition temperature of the amorphous components. J Pharm Sci 92:2495-2501. (Pubitemid 37484776)
    • (2003) Journal of Pharmaceutical Sciences , vol.92 , Issue.12 , pp. 2495-2501
    • Fitzpatrick, S.1    Saklatvala, R.2
  • 20
    • 0034001717 scopus 로고    scopus 로고
    • Optimization of storage stability of lyophilized actin using combinations of disaccharides and dextran
    • DOI 10.1002/(SICI)1520-6017(200002)89:2<199::AID-JPS7>3.0.CO;2-B
    • Allison SD, Manning MC, Randolph TW, Middleton K, Davis A, Carpenter JF. 2000. Optimization of storage stability of lyophilized actin using combinations of disaccharides and dextran. J Pharm Sci 89:199-214. (Pubitemid 30120800)
    • (2000) Journal of Pharmaceutical Sciences , vol.89 , Issue.2 , pp. 199-214
    • Allison, S.D.1    Manning, M.C.2    Randolph, T.W.3    Middleton, K.4    Davis, A.5    Carpenter, J.F.6
  • 21
    • 0034473318 scopus 로고    scopus 로고
    • The infrared absorption of amino acid side chains
    • DOI 10.1016/S0079-6107(00)00021-3, PII S0079610700000213
    • Barth A. 2000. The infrared absorption of amino acid side chains. Prog Biophys Mol Biol 74:141-173. (Pubitemid 32168153)
    • (2000) Progress in Biophysics and Molecular Biology , vol.74 , Issue.3-5 , pp. 141-173
    • Barth, A.1
  • 22
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • Barth A, Zscherp C. 2002. What vibrations tell us about proteins. Q Rev Biophys 35:369-430.
    • (2002) Q Rev Biophys , vol.35 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 23
    • 0028529836 scopus 로고
    • Studies on spectra/structure correlations in near-infrared spectra of proteins and polypeptides. Part I: A marker band for hydrogen bonds
    • Liu Y, Cho RK, Sakurai K, Miura T, Ozaki Y. 1994. Studies on spectra/structure correlations in near-infrared spectra of proteins and polypeptides. Part I: A marker band for hydrogen bonds. Appl Spectrosc 48:1249-1254.
    • (1994) Appl Spectrosc , vol.48 , pp. 1249-1254
    • Liu, Y.1    Cho, R.K.2    Sakurai, K.3    Miura, T.4    Ozaki, Y.5
  • 24
    • 0022013723 scopus 로고
    • Concerning the miscibility of poly(vinlylphenol) blends-FTIR study
    • Moskala EJ, Varnell DF, Coleman MM. 1985. Concerning the miscibility of poly(vinlylphenol) blends-FTIR study. Polymer 26:228-234.
    • (1985) Polymer , vol.26 , pp. 228-234
    • Moskala, E.J.1    Varnell, D.F.2    Coleman, M.M.3
  • 25
    • 1542609186 scopus 로고    scopus 로고
    • FTIR study of state and phase transitions of low moisture sucrose and lactose
    • DOI 10.1016/S0008-6215(03)00342-2, PII S0008621503003422
    • Ottenhof MA, MacNaughtan W, Farhat IA. 2003. FTIR study of state and phase transitions of low moisture sucrose and lactose. Carbohydr Res 338:2195-2202. (Pubitemid 38352682)
    • (2003) Carbohydrate Research , vol.338 , Issue.21 , pp. 2195-2202
    • Ottenhof, M.-A.1    MacNaughtan, W.2    Farhat, I.A.3
  • 26
    • 68949110967 scopus 로고    scopus 로고
    • US Patent 6,982,080 January 3, Hydroxyethyl starch - Containing polypeptide compositions
    • Warne NW, Koval RL, Carpenter JF, Randolph TW, Chongpraset S. US Patent 6,982,080 January 3, 2006. Hydroxyethyl starch - Containing polypeptide compositions.
    • (2006)
    • Warne, N.W.1    Koval, R.L.2    Carpenter, J.F.3    Randolph, T.W.4    Chongpraset, S.5
  • 28
    • 0034684214 scopus 로고    scopus 로고
    • Infrared spectra of amide groups in alpha-helical proteins: Evidence for hydrogen bonding between helices and water
    • DOI 10.1021/ja001782z
    • Manas ES, Getahun Z, Wright WW, DeGrado WF, Vanderkooi JM. 2000. Infrared spectra of amide groups in alpha-helical proteins: Evidence for hydrogen bonding between helices and water. J Am Chem Soc 122:9883-9890. (Pubitemid 30796215)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.41 , pp. 9883-9890
    • Manas, E.S.1    Getahun, Z.2    Wright, W.W.3    Degrado, W.F.4    Vanderkooi, J.M.5
  • 29
    • 1542275162 scopus 로고    scopus 로고
    • Protection of protein secondary structure by saccharides of different molecular weights during freeze-drying
    • DOI 10.1248/cpb.52.199
    • Izutsu K, Aoyagi N, Kojima S. 2004. Protection of protein secondary structure by saccharides of different molecular weights furing freeze-drying. Chem Pharm Bull 52:199-203. (Pubitemid 41656751)
    • (2004) Chemical and Pharmaceutical Bulletin , vol.52 , Issue.2 , pp. 199-203
    • Izutsu, K.-I.1    Aoyagi, N.2    Kojima, S.3
  • 31
    • 0036902487 scopus 로고    scopus 로고
    • Protein-trehalose-water structure in trehalose coated carboxymyoglobin
    • Cottone G, Ciccotti G, Cordone L. 2002. Protein-trehalose-water structure in trehalose coated carboxymyoglobin. J Chem Phys 117:9862-9866.
    • (2002) J Chem Phys , vol.117 , pp. 9862-9866
    • Cottone, G.1    Ciccotti, G.2    Cordone, L.3
  • 32
    • 0035144443 scopus 로고    scopus 로고
    • Molecular dynamics simulation of carboxy-myoglobin embedded in a trehalose-water matrix
    • Cottone G, Cordone L, Ciccotti G. 2001. Molecular dynamics simulation of carboxy-myoglobin embedded in a trehalose-water matrix. Biophys J 80:931-938. (Pubitemid 32128344)
    • (2001) Biophysical Journal , vol.80 , Issue.2 , pp. 931-938
    • Cottone, G.1    Cordone, L.2    Ciccotti, G.3
  • 33
    • 0025817772 scopus 로고
    • Cryoprotective effect of saccharides on denaturation of catalase by freeze-drying
    • Tanaka K, Takeda T, Miyajima K. 1991. Cryoprotective effect of saccharides on denaturation of catalase by freeze-drying. Chem Pharm Bull 39:1091-1094.
    • (1991) Chem Pharm Bull , vol.39 , pp. 1091-1094
    • Tanaka, K.1    Takeda, T.2    Miyajima, K.3
  • 34
    • 0033959890 scopus 로고    scopus 로고
    • Phase separation of polyelectrolytes and non-ionic polymers in frozen solutions
    • Izutsu K, Kojima S. 2000b. Phase separation of polyelectrolytes and non-ionic polymers in frozen solutions Phys Chem Chem Phys 2, 123-127.
    • (2000) Phys Chem Chem Phys , vol.2 , pp. 123-127
    • Izutsu, K.1    Kojima, S.2
  • 37
    • 0034825494 scopus 로고    scopus 로고
    • Molecular simulation of sucrose solutions near the glass transition temperature
    • Ekdawi-Server NC, Conrad PB, de Pablo JJ. 2001. Molecular simulation of sucrose solution near the glass transition temperature. J Phys Chem A 105:734-742. (Pubitemid 33764890)
    • (2001) Journal of Physical Chemistry A , vol.105 , Issue.4 , pp. 734-742
    • Ekdawi-Sever, N.C.1    Conrad, P.B.2    De Pablo, J.J.3
  • 38
    • 6344281045 scopus 로고    scopus 로고
    • Structure-Dynamics coupling between protein and external matrix in sucrose-coated and trehalose-coated MbCO: An FTIR study
    • Giuffrida S, Cottone G, Cordone L. 2004. Structure-Dynamics coupling between protein and external matrix in sucrose-coated and trehalose-coated MbCO: An FTIR study. J Phys Chem B 108:15415-15421.
    • (2004) J Phys Chem B , vol.108 , pp. 15415-15421
    • Giuffrida, S.1    Cottone, G.2    Cordone, L.3
  • 39
    • 0036498915 scopus 로고    scopus 로고
    • Molecular alloys formed by solid-state vitrification
    • DOI 10.1016/S0167-7322(01)00292-6, PII S0167732201002926
    • Nagahama M, Suge H. 2002. Molecular alloys formed by solid-state vitrification. J Mol Liquids 95:261-284. (Pubitemid 34167045)
    • (2002) Journal of Molecular Liquids , vol.95 , Issue.3 , pp. 261-284
    • Nagahama, M.1    Suga, H.2
  • 40
    • 0041397247 scopus 로고
    • 2nd-Order transition temperatures and related properties of polystyrene. 1. Influence of molecular weight
    • Fox TG, Flory PJ. 1950. 2nd-Order transition temperatures and related properties of polystyrene. 1. influence of molecular weight. J Appl Phys 21:581-591.
    • (1950) J Appl Phys , vol.21 , pp. 581-591
    • Fox, T.G.1    Flory, P.J.2
  • 41
    • 0030961777 scopus 로고    scopus 로고
    • Effect of glass transition temperature on the stability of lyophilized formulations containing a chimeric therapeutic monoclonal antibody
    • DOI 10.1023/A:1012144810067
    • Duddu SP, Dal Monte PR. 1997. Effect of glass transition temperature on the stability of lyophilized formulations containing a chimeric therapeutic monoclonal antibody. Pharm Res 14:591-595. (Pubitemid 27220275)
    • (1997) Pharmaceutical Research , vol.14 , Issue.5 , pp. 591-595
    • Duddu, S.P.1    Dal Monte, P.R.2
  • 42
    • 0001419585 scopus 로고    scopus 로고
    • Analysis and characterization of unusual ternary polymer miscibility in poly(ether diphenyl ether ketone), poly(ether ether ketone), and poly(ether imide)
    • Woo EM, Tseng YC. 2000. Analysis and characterization of unusual ternary polymer miscibility in poly(ether diphenyl ether ketone), poly(ether ether ketone), and poly(ether imide). Macromol Chem Phys 201:1877-1886.
    • (2000) Macromol Chem Phys , vol.201 , pp. 1877-1886
    • Woo, E.M.1    Tseng, Y.C.2
  • 43
    • 0034148934 scopus 로고    scopus 로고
    • Miscibility studies of binary and ternary mixtures of tactic poly(methyl methacrylates) with poly(vinylidene chloride-co-acrylonitrile)
    • DOI 10.1002/(SICI)1097-4628(20000307)75:10<1313::AID-APP13>3.0. CO;2-Z
    • Hsu WP, Yeh CF. 2000. Miscibility studies of binary and ternary mixtures of tactic poly(methyl methacrylates) with poly(vinylidene chloride-co- acrylonitrile). J Appl Polym Sci 75:1313-1321. (Pubitemid 32211551)
    • (2000) Journal of Applied Polymer Science , vol.75 , Issue.10 , pp. 1313-1321
    • Hsu, W.-P.1    Yeh, C.-F.2
  • 44
    • 0023825731 scopus 로고
    • Approach to the composition dependence of the glass-transition temperature of compatible polymer blends.1
    • Brekner MJ, Schneider HA, Cantow HJ. 1988. Approach to the composition dependence of the glass-transition temperature of compatible polymer blends.1. Polymer 29:78-85.
    • (1988) Polymer , vol.29 , pp. 78-85
    • Brekner, M.J.1    Schneider, H.A.2    Cantow, H.J.3
  • 45
    • 0024667113 scopus 로고
    • Glass-transition behavior of compatible polymer blends
    • Schneider HA. 1989. Glass-transition behavior of compatible polymer blends. Polymer 30:771-779.
    • (1989) Polymer , vol.30 , pp. 771-779
    • Schneider, H.A.1
  • 46
    • 0032204428 scopus 로고    scopus 로고
    • Functional group accessibility in hydrogen-bonded polymer blends. 3. Steric shielding effects
    • Pehlert GJ, Painter PC, Coleman MM. 1998. Functional group accessibility in hydrogen-bonded polymer blends. 3. Steric shielding effects. Macromolecules 31:8423-8424.
    • (1998) Macromolecules , vol.31 , pp. 8423-8424
    • Pehlert, G.J.1    Painter, P.C.2    Coleman, M.M.3
  • 47
    • 1442333169 scopus 로고    scopus 로고
    • Effect of steric hindrance on hydrogen-bonding interaction between polyesters and natural polyphenol catechin
    • Zhu B, Li JC, He Y, Yamane H, Kimura Y, Nishida H, Inoue Y. 2004. Effect of steric hindrance on hydrogen-bonding interaction between polyesters and natural polyphenol catechin. J Appl Polym Sci 91:3565-3573. (Pubitemid 38287212)
    • (2004) Journal of Applied Polymer Science , vol.91 , Issue.6 , pp. 3565-3573
    • Zhu, B.1    Li, J.2    He, Y.3    Yamane, H.4    Kimura, Y.5    Nishida, H.6    Inoue, Y.7
  • 48
    • 0037451183 scopus 로고    scopus 로고
    • Thermal properties and hydrogen bonding in polymer blend of polybenzoxazine/poly(N-vinyl-2-pyrrolidone)
    • DOI 10.1016/S0032-3861(02)00928-X, PII S003238610200928X
    • Su Y-C, Kuo S-W, Yei D-R, Xu H, Chang F-C. 2003. Thermal properties and hydrogen bonding in polymer blend of polybenzoxazine/poly(N-vinyl-2-pyrrolidone) . Polymer 44:2187-2191. (Pubitemid 36362330)
    • (2003) Polymer , vol.44 , Issue.8 , pp. 2187-2191
    • Su, Y.-C.1    Kuo, S.-W.2    Yei, D.-R.3    Xu, H.4    Chang, F.-C.5
  • 49
    • 0035876071 scopus 로고    scopus 로고
    • Study of hydrogen bonding strength in poly (epsilon-caprolactone) blends by DSC and FTIR
    • Kuo SW, Huang CF, Chang FC. 2001. Study of hydrogen bonding strength in poly (epsilon-caprolactone) blends by DSC and FTIR. J Polym Sci B Polym Phys 39:1348-1359.
    • (2001) J Polym Sci B Polym Phys , vol.39 , pp. 1348-1359
    • Kuo, S.W.1    Huang, C.F.2    Chang, F.C.3
  • 50
    • 0033221896 scopus 로고    scopus 로고
    • Hydrogen bonding in polyamide toughened novolac type phenolic resin
    • Wang FY, Ma CCM, Wu HD. 1999. Hydrogen bonding in polyamide toughened novolac type phenolic resin. J Appl Polym Sci 74:2283-2289.
    • (1999) J Appl Polym Sci , vol.74 , pp. 2283-2289
    • Wang, F.Y.1    Ccm, M.2    Wu, H.D.3
  • 51
    • 0034643864 scopus 로고    scopus 로고
    • Thermal behavior of native and hydrophobized wheat gluten, gliadin and glutenin-rich fractions by modulated DSC
    • DOI 10.1016/S0141-8130(00)00122-7, PII S0141813000001227
    • Micard V, Guilbert S. 2000. Thermal behavior of native and hydrophobized wheat gluten, gliadin, and glutenin-rich fractions by modulated DSC. Int J Biol Macromol 27:229-236. (Pubitemid 30316294)
    • (2000) International Journal of Biological Macromolecules , vol.27 , Issue.3 , pp. 229-236
    • Micard, V.1    Guilbert, S.2
  • 52
    • 0033770706 scopus 로고    scopus 로고
    • Thermal properties of raw and processed wheat gluten in relation with protein aggregation
    • PII S003238610000358X
    • Micard V, Morel MH, Bonicel J, Guilbert S. 2001. Thermal properties of raw and processed wheat gluten in relation with protein aggregation. Polymer 42:477-485. (Pubitemid 33717555)
    • (2001) Polymer , vol.42 , Issue.2 , pp. 477-485
    • Micard, V.1    Morel, M.-H.2    Bonicel, J.3    Guilbert, S.4
  • 53
    • 4243167095 scopus 로고
    • A classical thermodynamic discussion of the effect of composition on glass-transition temperatures
    • Couchman PR, Karasz FE. 1978. A classical thermodynamic discussion of the effect of composition on glass-transition temperatures. Macromolecules 11:117-119.
    • (1978) Macromolecules , vol.11 , pp. 117-119
    • Couchman, P.R.1    Karasz, F.E.2
  • 55
    • 0027115157 scopus 로고
    • Relationship between the glass transition temperature and the interaction parameter of miscible binary polymer blends
    • Lu X, Weiss RA. 1992. Relationship between the glass-transition temperature and the interaction parameter of miscible binary polymer blends. Macromolecules 25:3242-3246. (Pubitemid 23644983)
    • (1992) Macromolecules , vol.25 , Issue.12 , pp. 3242-3246
    • Lu, X.1    Weiss, R.A.2
  • 57
    • 33750901837 scopus 로고    scopus 로고
    • Changes in vibrational modes of water and bioprotectants in solution
    • DOI 10.1016/j.bpc.2006.07.003, PII S0301462206002353
    • Maguzù S, Migliardo F, Ramirez-Cuesta AJ. 2007. Changes in vibrational modes of water and bioprotectants in solution. Biophys Chem 125:138-142. (Pubitemid 44724896)
    • (2007) Biophysical Chemistry , vol.125 , Issue.1 , pp. 138-142
    • Magazu, S.1    Migliardo, F.2    Ramirez-Cuesta, A.J.3
  • 59
    • 0031239857 scopus 로고    scopus 로고
    • Manipulation of lyophilization-induced phase separation: Implications for pharmaceutical proteins
    • Heller MC, Carpenter JF, Randolph TW. 1997. Manipulation of lyophilization-induced phase separation: Implications for pharmaceutical proteins. Biotechnol Prog 13:590-596.
    • (1997) Biotechnol Prog , vol.13 , pp. 590-596
    • Heller, M.C.1    Carpenter, J.F.2    Randolph, T.W.3
  • 60
    • 0033558793 scopus 로고    scopus 로고
    • Application of a thermodynamic model to the prediction of phase separations in freeze-concentrated formulations for protein lyophilization
    • Heller MC, Carpenter JF, Randolph TW. 1999. Application of a thermodynamic model to the prediction of phase separations in freeze-concentrated formulations for protein lyophilization. Arch Biochem Biophys 363:191-201.
    • (1999) Arch Biochem Biophys , vol.363 , pp. 191-201
    • Heller, M.C.1    Carpenter, J.F.2    Randolph, T.W.3
  • 61
    • 0001343089 scopus 로고    scopus 로고
    • Freezing- and drying-induced perturbations of protein structure and mechanisms of protein protection by stabilizing additives
    • Rey L, May JC, editors. New York: Marcel Dekker, Inc.
    • Carpenter JF, Izutsu K, Randolph TW. 1999. Freezing- and drying-induced perturbations of protein structure and mechanisms of protein protection by stabilizing additives. In: Rey L, May JC, editors. Freeze-drying/lyophilization of pharmaceutical and biological products. New York: Marcel Dekker, Inc. pp 123-160.
    • (1999) Freeze-drying/lyophilization of Pharmaceutical and Biological Products , pp. 123-160
    • Carpenter, J.F.1    Izutsu, K.2    Randolph, T.W.3
  • 62
    • 28844441669 scopus 로고    scopus 로고
    • Calorimetric and structural investigations of the interaction between bovine serum albumin and high molecular weight dextran in water
    • Antonov YA, Wolf BA. 2005. Calorimetric and structural investigations of the interaction between bovine serum albumin and high molecular weight dextran in water. Biomacromolecules 6:2980-2989.
    • (2005) Biomacromolecules , vol.6 , pp. 2980-2989
    • Antonov, Y.A.1    Wolf, B.A.2
  • 64
    • 0035960794 scopus 로고    scopus 로고
    • Protein-induced changes in poly(ethylene glycol) brushes: Molecular weight and temperature dependence
    • DOI 10.1021/la010405c
    • Efremova NV, Sheth SR, Leckband DE. 2001. Protein-induced changes in poly(ethylene glycol) brushes: Molecular weight and temperature dependence. Langmuir 17:7628-7636. (Pubitemid 35331001)
    • (2001) Langmuir , vol.17 , Issue.24 , pp. 7628-7636
    • Efremova, N.V.1    Sheth, S.R.2    Leckband, D.E.3
  • 65
    • 2342427533 scopus 로고    scopus 로고
    • Mean-Square Displacement Relationship in Bioprotectant Systems by Elastic Neutron Scattering
    • Maguzù S, Maisano G, Migliardo F, Mondelli C. 2004. Mean-square displacement relationship in bioprotectant systems by elastic neutron scattering. Biophys J 86:3241-3249. (Pubitemid 38559000)
    • (2004) Biophysical Journal , vol.86 , Issue.5 , pp. 3241-3249
    • Magazu, S.1    Maisano, G.2    Migliardo, F.3    Mondelli, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.