메뉴 건너뛰기




Volumn 88, Issue 2, 1999, Pages 166-173

On the structural preservation of recombinant human growth hormone in a dried film of a synthetic biodegradable polymer

Author keywords

[No Author keywords available]

Indexed keywords

DICHLOROMETHANE; HUMAN GROWTH HORMONE; POLYGLACTIN; TREHALOSE;

EID: 0032970303     PISSN: 00223549     EISSN: None     Source Type: Journal    
DOI: 10.1021/js980272o     Document Type: Article
Times cited : (40)

References (67)
  • 1
    • 0001811050 scopus 로고    scopus 로고
    • Controlled drug delivery
    • Park, K., Ed.; American Chemical Society: Washington, DC
    • Robinson, J. R. Controlled drug delivery. In Controlled Drug Delivery. Challenges and Strategies; Park, K., Ed.; American Chemical Society: Washington, DC, 1997; pp 1-7.
    • (1997) Controlled Drug Delivery. Challenges and Strategies , pp. 1-7
    • Robinson, J.R.1
  • 2
    • 85030358539 scopus 로고
    • Protein stability grows in importance as more biodrugs enter clinicals
    • March 15
    • Pramik, M. J. Protein stability grows in importance as more biodrugs enter clinicals. Chem. Eng. News 1995, March 15.
    • (1995) Chem. Eng. News
    • Pramik, M.J.1
  • 3
    • 0002206469 scopus 로고    scopus 로고
    • Formulations and delivery of proteins and peptides: Design and development strategies
    • Cleland, J. L., Langer, R., Eds.; ACS Symposium Series, ACS Books
    • Cleland, J. L.; Langer, R. Formulations and Delivery of Proteins and Peptides: Design and Development Strategies. In Formulation and delivery of proteins and peptides; Cleland, J. L., Langer, R., Eds.; ACS Symposium Series, ACS Books; pp 1-19.
    • Formulation and Delivery of Proteins and Peptides , pp. 1-19
    • Cleland, J.L.1    Langer, R.2
  • 4
    • 0344490904 scopus 로고    scopus 로고
    • Site-specific drug delivery in the gastrointestinal tract
    • Park, K., Ed.; American Chemical Society: Washington, DC
    • Mrsny, R. J. Site-specific drug delivery in the gastrointestinal tract. In Controlled Drug Delivery. Challenges and Strategies; Park, K., Ed.; American Chemical Society: Washington, DC, 1997; pp 107-123.
    • (1997) Controlled Drug Delivery. Challenges and Strategies , pp. 107-123
    • Mrsny, R.J.1
  • 5
    • 0345876463 scopus 로고    scopus 로고
    • The pharmaceutical development of insulin. Historical perspectives and future directions
    • Shahrokh, Z.; Sluzky, V., Cleland, J. L., Shire, S. J., Randolph, T. W., Eds.; American Chemical Society: Washington, DC
    • Costantino, H. R.; Liauw, S.; Mitragotri, S.; Langer, R.; Klibanov, A. M.; Sluzky, V. The pharmaceutical development of insulin. Historical perspectives and future directions. In Therapeutic Protein and Peptide Formulation and Delivery; Shahrokh, Z.; Sluzky, V., Cleland, J. L., Shire, S. J., Randolph, T. W., Eds.; American Chemical Society: Washington, DC, 1997; pp 29-66.
    • (1997) Therapeutic Protein and Peptide Formulation and Delivery , pp. 29-66
    • Costantino, H.R.1    Liauw, S.2    Mitragotri, S.3    Langer, R.4    Klibanov, A.M.5    Sluzky, V.6
  • 6
    • 0025047522 scopus 로고
    • New methods of drug delivery
    • Langer, R. New methods of drug delivery. Science 1990, 249, 1527-1533.
    • (1990) Science , vol.249 , pp. 1527-1533
    • Langer, R.1
  • 7
    • 0029540462 scopus 로고
    • Biomaterials and biomedical engineering
    • Langer, R. Biomaterials and biomedical engineering. Chem. Eng. Sci. 1995, 50, 4109-4121.
    • (1995) Chem. Eng. Sci. , vol.50 , pp. 4109-4121
    • Langer, R.1
  • 8
    • 0000958535 scopus 로고    scopus 로고
    • Peptide, protein, and vaccine delivery from implantable polymeric systems. Progress and challenges
    • Challenges and Strategies Park. K., Ed.; American Chemical Society: Washington, DC
    • Schwendeman, S. P.; Costantino, H. R.; Gupta, R. K.; Langer, R. Peptide, protein, and vaccine delivery from implantable polymeric systems. Progress and challenges. In Controlled Drug Delivery. Challenges and Strategies; Park. K., Ed.; American Chemical Society: Washington, DC, 1997; pp 229-267.
    • (1997) Controlled Drug Delivery , pp. 229-267
    • Schwendeman, S.P.1    Costantino, H.R.2    Gupta, R.K.3    Langer, R.4
  • 9
    • 85030357237 scopus 로고    scopus 로고
    • 8]
    • 8].
  • 10
    • 0028853109 scopus 로고
    • Modeling monomer release from bioerodible polymers
    • Göpferich, A.; Langer, R. Modeling monomer release from bioerodible polymers. J. Controlled Release 1995, 33, 55-69.
    • (1995) J. Controlled Release , vol.33 , pp. 55-69
    • Göpferich, A.1    Langer, R.2
  • 11
    • 0031474199 scopus 로고    scopus 로고
    • A theoretical model of erosion and macromolecular drug release from biodegrading microspheres
    • Batycky, R. P.; Hanes, J.; Langer, R.; Edwards, D. A. A theoretical model of erosion and macromolecular drug release from biodegrading microspheres. J. Pharm. Sci. 1997, 86, 1464-1477.
    • (1997) J. Pharm. Sci. , vol.86 , pp. 1464-1477
    • Batycky, R.P.1    Hanes, J.2    Langer, R.3    Edwards, D.A.4
  • 12
    • 0002874721 scopus 로고    scopus 로고
    • Particle engineering of biodegradable colloids for site-specific drug delivery
    • Park, K., Ed.; American Chemical Society: Washington, DC
    • Scholes, P. D.; Coombes, A. G. A.; Davies, M. C.; Ilium, L.; Davis, S. S. Particle engineering of biodegradable colloids for site-specific drug delivery. In Controlled Drug Delivery. Challenges and Strategies; Park, K., Ed.; American Chemical Society: Washington, DC, 1997; pp 73-106.
    • (1997) Controlled Drug Delivery. Challenges and Strategies , pp. 73-106
    • Scholes, P.D.1    Coombes, A.G.A.2    Davies, M.C.3    Ilium, L.4    Davis, S.S.5
  • 15
    • 0002643399 scopus 로고    scopus 로고
    • Minimizing protein inactivation
    • Creighton, T., Ed.; Oxford University: New York
    • Volkin, D. B.; Klibanov, A. M. Minimizing protein inactivation. In Protein Function: A Practical Approach; Creighton, T., Ed.; Oxford University: New York, pp 1-24.
    • Protein Function: A Practical Approach , pp. 1-24
    • Volkin, D.B.1    Klibanov, A.M.2
  • 18
    • 0029278809 scopus 로고
    • Assessing the structural integrity of a lyophilized protein in organic solvents
    • Desai, U. R.; Klibanov, A. M. Assessing the structural integrity of a lyophilized protein in organic solvents. J. Am. Chem. Soc. 1995, 117, 3940-3945.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 3940-3945
    • Desai, U.R.1    Klibanov, A.M.2
  • 19
    • 0029902287 scopus 로고    scopus 로고
    • On protein denaturation in aqueous - Organic mixtures but not in pure organic solvents
    • Griebenow, K.; Klibanov, A. M. On protein denaturation in aqueous - organic mixtures but not in pure organic solvents. J. Am. Chem. Soc. 1996, 118, 11695-11700.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11695-11700
    • Griebenow, K.1    Klibanov, A.M.2
  • 20
    • 9544258376 scopus 로고    scopus 로고
    • Effect of high shear on proteins
    • Maa, Y.-F.; Hsu, C. C. Effect of high shear on proteins. Biotechnol. Bioeng. 1996, 51, 458-465.
    • (1996) Biotechnol. Bioeng. , vol.51 , pp. 458-465
    • Maa, Y.-F.1    Hsu, C.C.2
  • 21
    • 0026004620 scopus 로고
    • Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces
    • Sluzky, V.; Tamada, J. A.; Klibanov, A. M.; Langer, R. Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces. Proc. Natl. Acad. Sci. U.S.A. 1991, 88, 9377-9381.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 9377-9381
    • Sluzky, V.1    Tamada, J.A.2    Klibanov, A.M.3    Langer, R.4
  • 22
    • 0027163348 scopus 로고
    • Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers
    • Prestrelski, S. J.; Tedischi, N.; Arakawa, T.; Carpenter, J. F. Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers. Biophys. J. 1993, 65, 661-671.
    • (1993) Biophys. J. , vol.65 , pp. 661-671
    • Prestrelski, S.J.1    Tedischi, N.2    Arakawa, T.3    Carpenter, J.F.4
  • 23
    • 0028029812 scopus 로고
    • Protein structure in the lyophilized state: A hydrogen isotope exchange/NMR study with bovine pancreatic trypsin inhibitor
    • Desai, U. R., Osterhout, J. J.; Klibanov, A. M. Protein structure in the lyophilized state: a hydrogen isotope exchange/NMR study with bovine pancreatic trypsin inhibitor. J. Am. Chem. Soc. 1994, 116, 9420-9422.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 9420-9422
    • Desai, U.R.1    Osterhout, J.J.2    Klibanov, A.M.3
  • 24
    • 0028916150 scopus 로고
    • Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation
    • Dong, A.; Prestrelski, S. J.; Allison, S. D.; Carpenter, J. F. Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation. J. Pharm. Sci. 1995, 84, 415-424.
    • (1995) J. Pharm. Sci. , vol.84 , pp. 415-424
    • Dong, A.1    Prestrelski, S.J.2    Allison, S.D.3    Carpenter, J.F.4
  • 25
    • 0028847040 scopus 로고
    • Lyophilization-induced changes in the secondary structure of proteins
    • Griebenow, K.; Klibanov, A. M. Lyophilization-induced changes in the secondary structure of proteins. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 10969-10976.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 10969-10976
    • Griebenow, K.1    Klibanov, A.M.2
  • 26
    • 0026071674 scopus 로고
    • Moisture-induced aggregation of lyophilized proteins in the solid state
    • Liu, R.; Langer, R.; Klibanov, A. M. Moisture-induced aggregation of lyophilized proteins in the solid state. Biotechnol. Bioeng. 1991, 37, 177-184.
    • (1991) Biotechnol. Bioeng. , vol.37 , pp. 177-184
    • Liu, R.1    Langer, R.2    Klibanov, A.M.3
  • 27
    • 0028559724 scopus 로고
    • Solid-phase aggregation of proteins under pharmaceutically relevant conditions
    • Costantino, H. R.; Langer, R.; Klibanov, A. M. Solid-phase aggregation of proteins under pharmaceutically relevant conditions J. Pharm. Sci. 1994, 83, 1662-1669.
    • (1994) J. Pharm. Sci. , vol.83 , pp. 1662-1669
    • Costantino, H.R.1    Langer, R.2    Klibanov, A.M.3
  • 29
    • 0028875052 scopus 로고
    • Fourier transform infrared (FTIR) spectroscopic investigation of protein stability in the lyophilized form
    • Costantino, H. R.; Griebenow, K.; Mishra, P.; Langer, R.; Klibanov, A. M. Fourier transform infrared (FTIR) spectroscopic investigation of protein stability in the lyophilized form. Biochim. Biophys. Acta 1995, 253, 69-74.
    • (1995) Biochim. Biophys. Acta , vol.253 , pp. 69-74
    • Costantino, H.R.1    Griebenow, K.2    Mishra, P.3    Langer, R.4    Klibanov, A.M.5
  • 30
    • 0031734413 scopus 로고    scopus 로고
    • The effect of excipients on the structure and stability of lyophilized recombinant human growth hormone (rhGH)
    • Costantino, H. R.; Carrasquillo, K. G.; Cordero, R. A.; Mumenthaler, M.; Hsu, C. C.; Griebenow K. G. The effect of excipients on the structure and stability of lyophilized recombinant human growth hormone (rhGH). J. Pharm. Sci. 1998, 87, 1412-1420.
    • (1998) J. Pharm. Sci. , vol.87 , pp. 1412-1420
    • Costantino, H.R.1    Carrasquillo, K.G.2    Cordero, R.A.3    Mumenthaler, M.4    Hsu, C.C.5    Griebenow, K.G.6
  • 31
    • 85030353730 scopus 로고    scopus 로고
    • FTIR characterization of the secondary structure of proteins encapsulated within PLGA microspheres
    • in press
    • Fu, K.; Griebenow, K.; Hsieh, L.; Klibanov, A. M.; Langer, R. FTIR characterization of the secondary structure of proteins encapsulated within PLGA microspheres. J. Controlled Release, in press.
    • J. Controlled Release
    • Fu, K.1    Griebenow, K.2    Hsieh, L.3    Klibanov, A.M.4    Langer, R.5
  • 32
    • 0030588238 scopus 로고    scopus 로고
    • Effect of secondary structure on the activity of enzymes suspended in organic solvents
    • Dong, A.; Meyer, J. D.; Kendrick, B. S.; Manning, M. C.; Carpenter, J. F. Effect of secondary structure on the activity of enzymes suspended in organic solvents. Arch. Biochem. Biophys. 1996, 334, 406-414.
    • (1996) Arch. Biochem. Biophys. , vol.334 , pp. 406-414
    • Dong, A.1    Meyer, J.D.2    Kendrick, B.S.3    Manning, M.C.4    Carpenter, J.F.5
  • 33
    • 0342275236 scopus 로고    scopus 로고
    • Can conformational changes be responsible for solvent and excipient effects on the catalytic behavior of subtilisin Carlsberg in organic solvents?
    • Griebenow, K.; Klibanov, A. M. Can conformational changes be responsible for solvent and excipient effects on the catalytic behavior of subtilisin Carlsberg in organic solvents? Biotechnol. Bioeng. 1997, 53, 351-362.
    • (1997) Biotechnol. Bioeng. , vol.53 , pp. 351-362
    • Griebenow, K.1    Klibanov, A.M.2
  • 34
    • 0030964876 scopus 로고    scopus 로고
    • Preparation of excipient-free recombinant human tissue-type plasminogen activator by lyophilization from ammonium bicarbonate solution. An investigation of the two-stage sublimation phenomenon
    • Overcashier, D. E.; Brooks, D. A.; Costantino, H. R.; Hsu, C. C. Preparation of excipient-free recombinant human tissue-type plasminogen activator by lyophilization from ammonium bicarbonate solution. An investigation of the two-stage sublimation phenomenon. J. Pharm. Sci. 1997, 86, 455-459.
    • (1997) J. Pharm. Sci. , vol.86 , pp. 455-459
    • Overcashier, D.E.1    Brooks, D.A.2    Costantino, H.R.3    Hsu, C.C.4
  • 35
    • 0030319609 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy demonstrates that lyophilization alters the secondary structure of recombinant human growth hormone
    • Costantino, H. R.; Nguyen, T. H.; Hsu, C. C. Fourier transform infrared spectroscopy demonstrates that lyophilization alters the secondary structure of recombinant human growth hormone. Pharm. Sci. 1996, 2, 229-232.
    • (1996) Pharm. Sci. , vol.2 , pp. 229-232
    • Costantino, H.R.1    Nguyen, T.H.2    Hsu, C.C.3
  • 36
    • 0030028852 scopus 로고    scopus 로고
    • Aggregation of rhDNase occurred during the compression of KBr pellets used for FTIR spectroscopy
    • Chan, H.-K.; Ongpipattanakul, B.; Au-Yeung, J. Aggregation of rhDNase occurred during the compression of KBr pellets used for FTIR spectroscopy. Pharm. Res. 1996, 13, 238-242.
    • (1996) Pharm. Res. , vol.13 , pp. 238-242
    • Chan, H.-K.1    Ongpipattanakul, B.2    Au-Yeung, J.3
  • 37
    • 0031695133 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic investigation of the secondary structure of aqueous and dried recombinant human deoxyribonuclease I
    • Costantino, H. R.; Chen, B.; Griebenow, K.; Hsu, C. C.; Shire, S. J. Fourier transform infrared spectroscopic investigation of the secondary structure of aqueous and dried recombinant human deoxyribonuclease I. Pharm. Pharmacol. Commun. 1998, 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
  • 38
    • 0002663180 scopus 로고
    • Resolution enhancement of infrared spectra of biological systems
    • Clark, R. J. H.; Hester, R. E., Eds.; Wiley: New York
    • Mantsch, H. H.; Casal, H. L.; Jones, R. N. Resolution enhancement of infrared spectra of biological systems. In Spectroscopy of Biological Systems, Clark, R. J. H.; Hester, R. E., Eds.; Wiley: New York, 1986; pp 1-46.
    • (1986) Spectroscopy of Biological Systems , pp. 1-46
    • Mantsch, H.H.1    Casal, H.L.2    Jones, R.N.3
  • 39
    • 0022463740 scopus 로고
    • Resolution-enhanced Fourier transform infrared spectroscopy of enzymes
    • Susi, H.; Byler, D. M. Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Methods Enzymol. 1986, 130, 290-311.
    • (1986) Methods Enzymol. , vol.130 , pp. 290-311
    • Susi, H.1    Byler, D.M.2
  • 40
    • 0022691315 scopus 로고
    • Examination of the secondary structure on proteins by deconvoluted FTIR spectra
    • Byler, D. M.; Susi, H. Examination of the secondary structure on proteins by deconvoluted FTIR spectra. Biopolymers 1986, 25, 469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 41
    • 0027281270 scopus 로고
    • Secondary structure and temperature behavior of acetylcholinesterase. Studies by Fourier transform infrared spectroscopy
    • Görne-Tschelnokow, U.; Naumann, D.; Weise, C.; Hucho, F. Secondary structure and temperature behavior of acetylcholinesterase. Studies by Fourier transform infrared spectroscopy. Eur. J. Biochem. 1993, 213, 1235-1242.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 1235-1242
    • Görne-Tschelnokow, U.1    Naumann, D.2    Weise, C.3    Hucho, F.4
  • 42
    • 0023693897 scopus 로고
    • Structural and conformational changes of β-lactoglobulin B. An infrared spectroscopic study of the effect of pH and temperature
    • Casal, H. L.; Köhler, U.; Mantsch, H. H. Structural and conformational changes of β-lactoglobulin B. An infrared spectroscopic study of the effect of pH and temperature. Biochim. Biophys. Acta 1988, 957, 11-20.
    • (1988) Biochim. Biophys. Acta , vol.957 , pp. 11-20
    • Casal, H.L.1    Köhler, U.2    Mantsch, H.H.3
  • 43
    • 0027145627 scopus 로고
    • Investigation of secondary and tertiary structural changes of cytochrome c in complexes with anionic lipids using amide hydrogen exchange measurements. An FTIR study
    • Heimburg, T.; Marsh, D. Investigation of secondary and tertiary structural changes of cytochrome c in complexes with anionic lipids using amide hydrogen exchange measurements. An FTIR study. Biophys. J. 1993, 65, 2408-2417.
    • (1993) Biophys. J. , vol.65 , pp. 2408-2417
    • Heimburg, T.1    Marsh, D.2
  • 44
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor. Crystal structure of the complex
    • De Vos, A. M.; Ultsch, M.; Kossiakoff, A. A. Human growth hormone and extracellular domain of its receptor. Crystal structure of the complex. Science 1992, 255, 306-312.
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 45
    • 0029952769 scopus 로고    scopus 로고
    • Fourier transform IR spectroscopic study of hydration-induced structure changes in the solid state of ω-gliadins
    • Wellner, N.; Belton, P. S.; Tatham, A. S. Fourier transform IR spectroscopic study of hydration-induced structure changes in the solid state of ω-gliadins. Biochem. J. 1996, 319, 741-747.
    • (1996) Biochem. J. , vol.319 , pp. 741-747
    • Wellner, N.1    Belton, P.S.2    Tatham, A.S.3
  • 46
    • 0031058334 scopus 로고    scopus 로고
    • Effect of primary emulsions on microsphere size and protein-loading in the double emulsion process
    • Maa, Y.-F.; Hsu, C. C. Effect of primary emulsions on microsphere size and protein-loading in the double emulsion process. J. Microencap. 1997, 14, 225-241.
    • (1997) J. Microencap. , vol.14 , pp. 225-241
    • Maa, Y.-F.1    Hsu, C.C.2
  • 47
    • 85030355925 scopus 로고    scopus 로고
    • note
    • Note that the artificial creation of bands by inappropriate subtraction of the PLGA background is excluded by demonstrating that the amide IFTIR spectra of rhGH co-lyophilized with trehalose were practically identical when measured as KBr pellets or encapsulated in PLGA. Furthermore, the spectra were very similar to that in aqueous solution. See Materials and Methods for details of the method used to subtract the PLGA background.
  • 48
    • 14744285620 scopus 로고
    • Extraordinary stability of enzymes dried in trehalose: Simplified molecular biology
    • Colaço, C.; Sen, S.; Thangavelu, M.; Pinder, S.; Roser, B. Extraordinary stability of enzymes dried in trehalose: simplified molecular biology. Bio/Technology 1992, 10, 1007-1011.
    • (1992) Bio/Technology , vol.10 , pp. 1007-1011
    • Colaço, C.1    Sen, S.2    Thangavelu, M.3    Pinder, S.4    Roser, B.5
  • 49
    • 0024549238 scopus 로고
    • An infrared spectroscopic study of the interaction of carbohydrates with dried proteins
    • Carpenter, J. F.; Crowe, J. H. An infrared spectroscopic study of the interaction of carbohydrates with dried proteins. Biochemistry 1989, 28, 3916-3922.
    • (1989) Biochemistry , vol.28 , pp. 3916-3922
    • Carpenter, J.F.1    Crowe, J.H.2
  • 50
    • 0028151971 scopus 로고
    • IR and Raman spectroscopic studies of the interaction of trehalose with hen egg white lysozyme
    • Belton, P. S.; Gil, A. M. IR and Raman spectroscopic studies of the interaction of trehalose with hen egg white lysozyme. Biopolymers 1994, 34, 957-961.
    • (1994) Biopolymers , vol.34 , pp. 957-961
    • Belton, P.S.1    Gil, A.M.2
  • 52
    • 0024278258 scopus 로고
    • Enzymatic catalysis in nonaqueous solvents
    • Zaks, A.; Klibanov, A. M. Enzymatic catalysis in nonaqueous solvents. J. Biol. Chem. 1988, 263, 3194-3201.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3194-3201
    • Zaks, A.1    Klibanov, A.M.2
  • 53
    • 0024653016 scopus 로고
    • Enzymatic catalysis in anhydrous organic solvents
    • Klibanov, A. M. Enzymatic catalysis in anhydrous organic solvents. TIBS 1989, 14, 141-144.
    • (1989) TIBS , vol.14 , pp. 141-144
    • Klibanov, A.M.1
  • 54
    • 0031104802 scopus 로고    scopus 로고
    • Why are enzymes less active in organic solvents than in water?
    • Klibanov, A. M. Why are enzymes less active in organic solvents than in water? Trends Biotechnol. 1997, 15, 97-101.
    • (1997) Trends Biotechnol. , vol.15 , pp. 97-101
    • Klibanov, A.M.1
  • 55
    • 0029883864 scopus 로고    scopus 로고
    • The mechanistic dissection of the plunge in enzymatic activity upon transition from water to anhydrous solvents
    • Schmidtke, J. L.; Wescott, C. R.; Klibanov, A. M. The mechanistic dissection of the plunge in enzymatic activity upon transition from water to anhydrous solvents. J. Am. Chem. Soc. 1996, 118, 3360-3365.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3360-3365
    • Schmidtke, J.L.1    Wescott, C.R.2    Klibanov, A.M.3
  • 56
    • 0028928260 scopus 로고
    • What is remembered and why?
    • Klibanov, A. M. What is remembered and why? Nature 1995, 374, 596.
    • (1995) Nature , vol.374 , pp. 596
    • Klibanov, A.M.1
  • 57
    • 0030571576 scopus 로고    scopus 로고
    • Structural basis for the molecular memory of imprinted proteins in anhydrous media
    • Mishra, P.; Griebenow, K.; Klibanov, A. M. Structural basis for the molecular memory of imprinted proteins in anhydrous media. Biotechnol. Bioeng. 1996, 52, 609-614.
    • (1996) Biotechnol. Bioeng. , vol.52 , pp. 609-614
    • Mishra, P.1    Griebenow, K.2    Klibanov, A.M.3
  • 58
    • 0030908708 scopus 로고    scopus 로고
    • Controlling subtilisin activity and selectivity in organic media by imprinting with nucleophilic substrates
    • Rich, J. O.; Dordick, J. S. Controlling subtilisin activity and selectivity in organic media by imprinting with nucleophilic substrates. J. Am. Chem. Soc. 1997, 119, 3245-3252.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3245-3252
    • Rich, J.O.1    Dordick, J.S.2
  • 59
    • 0021763770 scopus 로고
    • Enzymatic catalysis in organic media at 100 °C
    • Zaks, A.; Klibanov, A. M. Enzymatic catalysis in organic media at 100 °C. Science 1984, 224, 1249-1251.
    • (1984) Science , vol.224 , pp. 1249-1251
    • Zaks, A.1    Klibanov, A.M.2
  • 61
    • 0027909364 scopus 로고
    • Solid-state nuclear magnetic resonance investigation of solvent dependence of tyrosyl ring motion in an enzyme
    • Burke, P. A.; Griffin, R. G.; Klibanov, A. M. Solid-state nuclear magnetic resonance investigation of solvent dependence of tyrosyl ring motion in an enzyme. Biotechnol. Bioeng. 1993, 42, 87-94.
    • (1993) Biotechnol. Bioeng. , vol.42 , pp. 87-94
    • Burke, P.A.1    Griffin, R.G.2    Klibanov, A.M.3
  • 62
    • 0026112863 scopus 로고
    • Activity and flexibility of alcohol dehydrogenase in organic solvents
    • Guinn, R. M.; Skerker, P. S.; Kavanaugh, P.; Clark, D. S. Activity and flexibility of alcohol dehydrogenase in organic solvents. Biotechnol. Bioeng. 1991, 37, 303-308.
    • (1991) Biotechnol. Bioeng. , vol.37 , pp. 303-308
    • Guinn, R.M.1    Skerker, P.S.2    Kavanaugh, P.3    Clark, D.S.4
  • 64
    • 0029560442 scopus 로고
    • Flexibility of enzymes suspended in organic solvents probed by time-resolved fluorescence anisotropy. Evidence that enzyme activity and enantioselectivity are directly related to enzyme flexibility
    • Broos, J.; Visser, A. J. W.; Engbersen, J. F. J.; Verboom, W.; van Hoek, A.; Reinhoudt, D. N. Flexibility of enzymes suspended in organic solvents probed by time-resolved fluorescence anisotropy. Evidence that enzyme activity and enantioselectivity are directly related to enzyme flexibility. J. Am. Chem. Soc. 1995, 117, 12657-12663.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 12657-12663
    • Broos, J.1    Visser, A.J.W.2    Engbersen, J.F.J.3    Verboom, W.4    Van Hoek, A.5    Reinhoudt, D.N.6
  • 65
    • 0001159492 scopus 로고
    • Protein dynamics and solvation in aqueous and nonaqueous environments
    • Hartsough, D. S.; Merz, K. M. Jr. Protein dynamics and solvation in aqueous and nonaqueous environments. J. Am. Chem. Soc. 1993, 115, 6529-6537.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 6529-6537
    • Hartsough, D.S.1    Merz K.M., Jr.2
  • 66
    • 0030662088 scopus 로고    scopus 로고
    • The concept of solvent compatibility and its impact on protein stability and activity enhancement in nonaqueous solvents
    • Toba, S.; Merz, K. M. Jr. The concept of solvent compatibility and its impact on protein stability and activity enhancement in nonaqueous solvents. J. Am. Chem. Soc. 1997, 119, 9939-9948.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 9939-9948
    • Toba, S.1    Merz K.M., Jr.2
  • 67
    • 0030853055 scopus 로고    scopus 로고
    • The lubrication of life: A proposal that solvent water promotes extremely fast conformational fluctuations in mobile heteropolymer structure
    • Barron, L. D.; Hecht, L.; Wilson, G. The lubrication of life: a proposal that solvent water promotes extremely fast conformational fluctuations in mobile heteropolymer structure. Biochemistry 1997, 36, 13143-13147.
    • (1997) Biochemistry , vol.36 , pp. 13143-13147
    • Barron, L.D.1    Hecht, L.2    Wilson, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.