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Volumn 4, Issue 8, 1998, Pages 391-395

Fourier-transform infrared spectroscopic investigation of the secondary structure of aqueous and dried recombinant human deoxyribonuclease I

Author keywords

[No Author keywords available]

Indexed keywords

DORNASE ALFA;

EID: 0031695133     PISSN: 14608081     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (14)

References (13)
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  • 2
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  • 3
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    • 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. (1996) Fourier-transform infrared spectroscopy demonstrates that lyophilization alters the secondary structure of recombinant human growth hormone. Pharm. Sci. 2: 229-232
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  • 4
    • 0031417508 scopus 로고    scopus 로고
    • Fourier-transform infrared spectroscopic analysis of the secondary structure of recombinant humanized immunoglobulin G
    • Costantino, H. R., Andya, J. D., Shire, S. J., Hsu, C. C. (1997) Fourier-transform infrared spectroscopic analysis of the secondary structure of recombinant humanized immunoglobulin G. Pharm. Sci. 3: 121-128
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  • 5
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    • Dong, A., Prestrelski, S. J., Allison, S. D., Carpenter, J. F. (1995) Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation. J. Pharm. Sci. 84: 415-424
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    • Dong, A.1    Prestrelski, S.J.2    Allison, S.D.3    Carpenter, J.F.4
  • 6
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    • Griebenow, K., Klibanov, A. M. (1995) Lyophilization-induced reversible changes in the secondary structure of proteins. Proc. Natl Acad. Sci USA 92: 10969-10976
    • (1995) Proc. Natl Acad. Sci USA , vol.92 , pp. 10969-10976
    • Griebenow, K.1    Klibanov, A.M.2
  • 7
    • 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. (1997) Can conformational changes be responsible for solvent and excipient effects on the catalytic behavior of subtilisin Carlsberg in organic solvents? Biotechnol. Bioeng. 53: 351-362
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  • 8
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    • Surface denaturation at solid-void interface. A possible pathway by which opalescent particulates form during the storage of lyophilized tissue-type plasminogen activator at high temperatures
    • Hsu, C. C., Nguyen, H. M., Yeung, D. A., Brooks, D. A., Kow, G. S., Bewley, T. A., Pearlman, R. (1995) Surface denaturation at solid-void interface. A possible pathway by which opalescent particulates form during the storage of lyophilized tissue-type plasminogen activator at high temperatures. Pharm. Res. 12: 69-77
    • (1995) Pharm. Res. , vol.12 , pp. 69-77
    • Hsu, C.C.1    Nguyen, H.M.2    Yeung, D.A.3    Brooks, D.A.4    Kow, G.S.5    Bewley, T.A.6    Pearlman, R.7
  • 9
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    • Replacing succinate with glycolate buffer improves the stability of lyophilized interferon-gamma
    • Lam, X. M., Costantino, H. R., Overcashier, D. E., Nguyen, T. H., Hsu C. C. (1996) Replacing succinate with glycolate buffer improves the stability of lyophilized interferon-gamma. Int. J. Pharm. 142: 85-95
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  • 10
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  • 11
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    • Shire, S. J. (1996) Stability characterization and formulation development of recombinant human deoxyribonuclease I (Pulmozyme,®(Dornase alpha)). In: Pearlman, R., Wang, Y. J. (eds) Formulation, Characterization and Stability of Protein Drugs. Plenum press, New York, pp 393-426
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.