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Volumn 44, Issue 2-3, 1997, Pages 255-261

Heterogeneity of serum albumin samples with respect to solid-state aggregation via thiol-disulfide interchange - Implications for sustained release from polymers

Author keywords

albumin; lyophilization; poly(fatty acid dimer:sebacic acid); thiol disulfide interchange

Indexed keywords

BOVINE SERUM ALBUMIN; DIMER; DISULFIDE; FATTY ACID; HUMAN SERUM ALBUMIN; POLYMER; RECOMBINANT ALBUMIN; SEBACIC ACID; SERUM ALBUMIN; THIOL; UNCLASSIFIED DRUG;

EID: 0031575559     PISSN: 01683659     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-3659(96)01528-3     Document Type: Article
Times cited : (15)

References (23)
  • 1
    • 0023803010 scopus 로고
    • The role of moisture in protein stability
    • M.J. Hageman, The role of moisture in protein stability. Drug Dev. Ind. Pharmacy 14 (1988) 2047-2070.
    • (1988) Drug Dev. Ind. Pharmacy , vol.14 , pp. 2047-2070
    • Hageman, M.J.1
  • 2
    • 0000652983 scopus 로고
    • Preformulation studies oriented toward sustained delivery of recombinant somatotropins
    • M.J. Hageman, J.M. Bauer, P.L. Possert and R.T. Darrington, Preformulation studies oriented toward sustained delivery of recombinant somatotropins. J. Agric. Food Chem. 40 (1992) 348-355.
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 348-355
    • Hageman, M.J.1    Bauer, J.M.2    Possert, P.L.3    Darrington, R.T.4
  • 3
    • 0026071674 scopus 로고
    • Moisture-induced aggregation of lyophilized proteins in the solid state
    • W.R. Liu, R. Langer and A.M. Klibanov, Moisture-induced aggregation of lyophilized proteins in the solid state. Biotechnol. Bioeng. 37 (1991) 177-184.
    • (1991) Biotechnol. Bioeng. , vol.37 , pp. 177-184
    • Liu, W.R.1    Langer, R.2    Klibanov, A.M.3
  • 4
    • 0028345740 scopus 로고
    • The aggregation of bovine serum albumin in solution and in the solid state
    • G.M. Jordan, S. Yoshioka and T. Terao, The aggregation of bovine serum albumin in solution and in the solid state. J. Pharm. Pharmacol. 46 (1994) 182-185.
    • (1994) J. Pharm. Pharmacol. , vol.46 , pp. 182-185
    • Jordan, G.M.1    Yoshioka, S.2    Terao, T.3
  • 5
    • 0027955039 scopus 로고
    • Moisture-induced aggregation of lyophilized insulin
    • H.R. Costantino, R. Langer and A.M. Klibanov, Moisture-induced aggregation of lyophilized insulin. Pharm. Res. 11 (1994) 21-29.
    • (1994) Pharm. Res. , vol.11 , pp. 21-29
    • Costantino, H.R.1    Langer, R.2    Klibanov, A.M.3
  • 6
    • 0029071504 scopus 로고
    • Aggregation of a lyophilized pharmaceutical protein, recombinant human albumin: Effect of moisture and stabilization by excipients
    • H.R. Costantino, R. Langer and A.M. Klibanov, Aggregation of a lyophilized pharmaceutical protein, recombinant human albumin: Effect of moisture and stabilization by excipients. Bio/Technology 13 (1995) 493-496.
    • (1995) Bio/Technology , vol.13 , pp. 493-496
    • Costantino, H.R.1    Langer, R.2    Klibanov, A.M.3
  • 7
    • 0028875052 scopus 로고
    • Fourier-transform infrared (FTIR) spectroscopic investigation of protein stability in the lyophilized form
    • H.R. Costantino, K. Griebenow, P. Mishra, R. Langer and A.M. Klibanov, Fourier-transform infrared (FTIR) spectroscopic investigation of protein stability in the lyophilized form. Biochim. Biophys. Acta 1253 (1995) 69-74.
    • (1995) Biochim. Biophys. Acta , vol.1253 , pp. 69-74
    • Costantino, H.R.1    Griebenow, K.2    Mishra, P.3    Langer, R.4    Klibanov, A.M.5
  • 8
    • 0028559724 scopus 로고
    • Solid-phase aggregation of proteins under pharmaceutically relevant conditions
    • H.R. Costantino, R. Langer and A.M. Klibanov, Solid-phase aggregation of proteins under pharmaceutically relevant conditions. J. Pharm. Sci. 83 (1995) 1662-1669.
    • (1995) J. Pharm. Sci. , vol.83 , pp. 1662-1669
    • Costantino, H.R.1    Langer, R.2    Klibanov, A.M.3
  • 9
    • 0002394569 scopus 로고
    • Polymers for the sustained release of macromolecules: Applications and control of release kinetics
    • R. Baker (Ed.) Academic Press, New York
    • R. Langer, W.D. Rhine, D.S.T. Hsieh and R.S. Bawa, Polymers for the sustained release of macromolecules: applications and control of release kinetics. In: R. Baker (Ed.), Controlled Release of Bioactive Materials, Academic Press, New York, 1980, pp. 83-98.
    • (1980) Controlled Release of Bioactive Materials , pp. 83-98
    • Langer, R.1    Rhine, W.D.2    Hsieh, D.S.T.3    Bawa, R.S.4
  • 11
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of serum albumin
    • X.M. He and D.C. Carter, Atomic structure and chemistry of serum albumin. Nature 358 (1992) 209-215.
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 12
    • 0022043805 scopus 로고
    • Polymers for the controlled release of macromolecules: Effect of molecular weight of ethylene-vinyl acetate copolymer
    • T. Hsu and R. Langer, Polymers for the controlled release of macromolecules: effect of molecular weight of ethylene-vinyl acetate copolymer. J. Biomat. Res. 19 (1985) 445-460.
    • (1985) J. Biomat. Res. , vol.19 , pp. 445-460
    • Hsu, T.1    Langer, R.2
  • 13
    • 0027574132 scopus 로고
    • Absorbable biopolymers derived from dimer fatty acids
    • A. Domb and M. Maniar, Absorbable biopolymers derived from dimer fatty acids. J. Polymer Sci. 31 (1993) 1275-1285.
    • (1993) J. Polymer Sci. , vol.31 , pp. 1275-1285
    • Domb, A.1    Maniar, M.2
  • 14
    • 0001425703 scopus 로고
    • The availability of disulfide bonds of human and bovine serum albumin and of bovine γ-globulin by thioglycolic acid
    • E. Katchalski, G.S. Benjamin and V. Gross, The availability of disulfide bonds of human and bovine serum albumin and of bovine γ-globulin by thioglycolic acid. J. Am. Chem. Soc. 79 (1957) 4096-4099.
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 4096-4099
    • Katchalski, E.1    Benjamin, G.S.2    Gross, V.3
  • 15
    • 0014216041 scopus 로고
    • Removal of fatty acids from serum albumin by charcoal treatment
    • R.F. Chen, Removal of fatty acids from serum albumin by charcoal treatment. J. Biol. Chem. 242 (1967) 173-181.
    • (1967) J. Biol. Chem. , vol.242 , pp. 173-181
    • Chen, R.F.1
  • 16
    • 0015326424 scopus 로고
    • Size and shape determination of native and defatted bovine serum albumin monomers. II. Influence of the fatty acid content on the conformation of bovine serum albumin monomers
    • (Tokyo)
    • F. Soetewey, M. Rosseneu-Motreff, R. Lamote and H. Peeters, Size and shape determination of native and defatted bovine serum albumin monomers. II. Influence of the fatty acid content on the conformation of bovine serum albumin monomers. J. Biochem. (Tokyo) 71 (1972) 705-710.
    • (1972) J. Biochem. , vol.71 , pp. 705-710
    • Soetewey, F.1    Rosseneu-Motreff, M.2    Lamote, R.3    Peeters, H.4
  • 17
    • 0026494225 scopus 로고
    • Analysis of the structure of fatty acid-free human serum albumin by tritium labeling
    • E.S. Dzhafarov, Analysis of the structure of fatty acid-free human serum albumin by tritium labeling. Mol. Biol. 26 (1992) 168-172.
    • (1992) Mol. Biol. , vol.26 , pp. 168-172
    • Dzhafarov, E.S.1
  • 18
    • 0011378026 scopus 로고
    • Inhibition of peptic digestion of serum albumin by fatty acids
    • J.A. Klapper and J.R. Cann, Inhibition of peptic digestion of serum albumin by fatty acids. Arch. Biochem. Biophys. 108 (1964) 531-534.
    • (1964) Arch. Biochem. Biophys. , vol.108 , pp. 531-534
    • Klapper, J.A.1    Cann, J.R.2
  • 19
    • 0014441134 scopus 로고
    • The microheterogeneity of plasma albumins (V): Permutations in disulfide pairings as a probable source of microheterogeneity in bovine albumin
    • M. Sogami, H.A. Petersen and J.F. Foster, The microheterogeneity of plasma albumins (V): Permutations in disulfide pairings as a probable source of microheterogeneity in bovine albumin. Biochemistry 8 (1969) 49-58.
    • (1969) Biochemistry , vol.8 , pp. 49-58
    • Sogami, M.1    Petersen, H.A.2    Foster, J.F.3
  • 20
    • 0017256207 scopus 로고
    • Heat denaturation of human serum albumin: Migration of fatty acids
    • J. Brandt and L.-O. Andersson, Heat denaturation of human serum albumin: migration of fatty acids. Int. J. Peptide Protein Res. 8 (1976) 33-37.
    • (1976) Int. J. Peptide Protein Res. , vol.8 , pp. 33-37
    • Brandt, J.1    Andersson, L.-O.2
  • 21
    • 0018112664 scopus 로고
    • Immunochemistry of bovine serum albumin
    • A.F.S.A. Habeeb, Immunochemistry of bovine serum albumin. Adv. Exp. Med. Biol. 98 (1978) 101-117.
    • (1978) Adv. Exp. Med. Biol. , vol.98 , pp. 101-117
    • Habeeb, A.F.S.A.1
  • 22
    • 0001851995 scopus 로고
    • Some aspects of the structure and conformational properties of serum albumin
    • V.M. Rosenoer, M. Oratz and M.A. Rothschild (Eds.) Pergamon, Oxford
    • J.F. Foster, Some aspects of the structure and conformational properties of serum albumin. In: V.M. Rosenoer, M. Oratz and M.A. Rothschild (Eds.), Albumin Structure, Function, and Uses, Pergamon, Oxford, 1977, pp. 53-84.
    • (1977) Albumin Structure, Function, and Uses , pp. 53-84
    • Foster, J.F.1
  • 23
    • 0026594794 scopus 로고
    • Brain biocompatibility of a biodegradable controlled release polymer consisting of anhydride polymer of fatty acid dimer and sebacic acid
    • H. Brem, A. Domb, D. Lenartz, C. Dureza, A. Olivi and J. Epstein, Brain biocompatibility of a biodegradable controlled release polymer consisting of anhydride polymer of fatty acid dimer and sebacic acid. J. Controlled Rel. 19 (1992) 325-330.
    • (1992) J. Controlled Rel. , vol.19 , pp. 325-330
    • Brem, H.1    Domb, A.2    Lenartz, D.3    Dureza, C.4    Olivi, A.5    Epstein, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.