메뉴 건너뛰기




Volumn 57, Issue 5, 2005, Pages 555-564

Stabilization of somatropin by heparin

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ARGININE; GLYCOSAMINOGLYCAN; HEPARIN; HISTIDINE; HUMAN GROWTH HORMONE; HYDROCORTISONE; HYDROCORTISONE SODIUM SUCCINATE; LEVOTHYROXINE; LYSINE; STABILIZING AGENT; TYROSINE;

EID: 17644386823     PISSN: 00223573     EISSN: None     Source Type: Journal    
DOI: 10.1211/0022357055975     Document Type: Article
Times cited : (9)

References (40)
  • 1
    • 0026071969 scopus 로고
    • Monitoring of protein conformation by high-performance size-exclusion liquid chromatography and scanning diode array second derivative UV absorption spectroscopy
    • Ackland, C. E., Berndt, W. G., Frezza, J. E., Landgraf, B. E., Pritchard, K. W., Ciardelli, T. (1991) Monitoring of protein conformation by high-performance size-exclusion liquid chromatography and scanning diode array second derivative UV absorption spectroscopy. J. Chromatogr. 540: 187-198
    • (1991) J. Chromatogr. , vol.540 , pp. 187-198
    • Ackland, C.E.1    Berndt, W.G.2    Frezza, J.E.3    Landgraf, B.E.4    Pritchard, K.W.5    Ciardelli, T.6
  • 2
    • 2442468760 scopus 로고    scopus 로고
    • Medical guidelines for clinical practice for growth hormone use in adults and children - 2003 Update
    • American Association of Clinical Endocrinologists (2003) Medical guidelines for clinical practice for growth hormone use in adults and children - 2003 update. Endocr. Pract. 9: 64-76
    • (2003) Endocr. Pract. , vol.9 , pp. 64-76
  • 5
    • 0021139068 scopus 로고
    • Conformational comparison of human pituitary growth hormone and human chorionic somatomammotropin (human placental lactogen) by second-order absorption spectroscopy
    • Bewley, T. A., Li, C. H. (1984) Conformational comparison of human pituitary growth hormone and human chorionic somatomammotropin (human placental lactogen) by second-order absorption spectroscopy. Arch. Biochem. Biophys. 233: 219-227
    • (1984) Arch. Biochem. Biophys. , vol.233 , pp. 219-227
    • Bewley, T.A.1    Li, C.H.2
  • 7
    • 0025215889 scopus 로고
    • Equilibrium denaturation of human growth-hormone and its cysteine-modified forms
    • Brems, D. N., Brown, P. L., Becker, G. W. (1990) Equilibrium denaturation of human growth-hormone and its cysteine-modified forms. J. Biol. Chem. 265: 5504-5511
    • (1990) J. Biol. Chem. , vol.265 , pp. 5504-5511
    • Brems, D.N.1    Brown, P.L.2    Becker, G.W.3
  • 8
    • 0024584913 scopus 로고
    • Molecular modeling of protein-glycosaminoglycan interactions
    • Cardin, A. D., Weintraub, H. J. R. (1989) Molecular modeling of protein-glycosaminoglycan interactions. Arteriosclerosis 9: 21-32
    • (1989) Arteriosclerosis , vol.9 , pp. 21-32
    • Cardin, A.D.1    Weintraub, H.J.R.2
  • 9
    • 0027228385 scopus 로고
    • Techniques for assessing the effects of pharmaceutical excipients on the aggregation of porcine growth hormone
    • Charman, S. A., Mason, K. L., Charman, W. N. (1993) Techniques for assessing the effects of pharmaceutical excipients on the aggregation of porcine growth hormone. Pharm. Res. 10: 954-962
    • (1993) Pharm. Res. , vol.10 , pp. 954-962
    • Charman, S.A.1    Mason, K.L.2    Charman, W.N.3
  • 10
    • 0028588599 scopus 로고
    • Strategies to suppress aggregation of recombinant keratinocyte growth-factor during liquid formulation development
    • Chen, B. L., Arakawa, T., Hsu, E., Narhi, L. O., Tressel, T. J., Chien, S. L. (1994) Strategies to suppress aggregation of recombinant keratinocyte growth-factor during liquid formulation development. J. Pharm. Sci. 83: 1657-1661
    • (1994) J. Pharm. Sci. , vol.83 , pp. 1657-1661
    • Chen, B.L.1    Arakawa, T.2    Hsu, E.3    Narhi, L.O.4    Tressel, T.J.5    Chien, S.L.6
  • 11
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • Chi, E. Y., Krishnan, S., Randolph, T. W., Carpenter, J. F. (2003) Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation. Pharm. Res. 20: 1325-1336
    • (2003) Pharm. Res. , vol.20 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 12
    • 0018231626 scopus 로고
    • Physiological function of connective tissue polysaccharides
    • Comper, W. D., Laurent, T. C. (1978) Physiological function of connective tissue polysaccharides. Physiol. Rev. 58: 255-315
    • (1978) Physiol. Rev. , vol.58 , pp. 255-315
    • Comper, W.D.1    Laurent, T.C.2
  • 14
    • 0027874299 scopus 로고
    • Characterization and formulation considerations for recombinantly derived bovine somatotropin
    • Pearlman, R. (ed.). Plenum Press, New York
    • Davio, S. R., Hageman, M. J. (1993) Characterization and formulation considerations for recombinantly derived bovine somatotropin. In: Pearlman, R. (ed.) Stability and characterization of protein and peptide drugs: case histories. Plenum Press, New York, pp 59-89
    • (1993) Stability and Characterization of Protein and Peptide Drugs: Case Histories , pp. 59-89
    • Davio, S.R.1    Hageman, M.J.2
  • 15
    • 0027502115 scopus 로고
    • Evidence for a self-associating equilibrium intermediate during folding of human growth hormone
    • DeFelippis, M. R., Alter, L. A., Pekar, A. H., Havel, H. A., Brems, D. N. (1992) Evidence for a self-associating equilibrium intermediate during folding of human growth hormone. Biochemistry 32: 1555-1562
    • (1992) Biochemistry , vol.32 , pp. 1555-1562
    • DeFelippis, M.R.1    Alter, L.A.2    Pekar, A.H.3    Havel, H.A.4    Brems, D.N.5
  • 17
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K. A. (1990) Dominant forces in protein folding. Biochemistry 29: 7133-7155
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 18
    • 0036888473 scopus 로고    scopus 로고
    • Biodegradable laminar implants for sustained release of recombinant human growth hormone
    • Garcia, J. T., Dorta, M. J., Munguia, O., Llabres, M., Farina, J. B. (2002) Biodegradable laminar implants for sustained release of recombinant human growth hormone. Biomaterials 23: 4759-4764
    • (2002) Biomaterials , vol.23 , pp. 4759-4764
    • Garcia, J.T.1    Dorta, M.J.2    Munguia, O.3    Llabres, M.4    Farina, J.B.5
  • 19
    • 0023352252 scopus 로고
    • Highly improved precision of the hypophysectomized female rat body weight gain bioassayl for growth hormone by increased frequency of injections, avoidance of antibody formation, and other simple modifications
    • Groesbeck, M. D., Parlow, A. F. (1987) Highly improved precision of the hypophysectomized female rat body weight gain bioassayl for growth hormone by increased frequency of injections, avoidance of antibody formation, and other simple modifications. Endocrinology 120: 2582-2590
    • (1987) Endocrinology , vol.120 , pp. 2582-2590
    • Groesbeck, M.D.1    Parlow, A.F.2
  • 20
    • 0022976484 scopus 로고
    • Reversible self-association of bovine growth hormone during equilibrium unfolding
    • Havel, H. A., Kauffman, E. W., Plaisted, S. M., Brems, D. N. (1986) Reversible self-association of bovine growth hormone during equilibrium unfolding. Biochemistry 25: 6533-6538
    • (1986) Biochemistry , vol.25 , pp. 6533-6538
    • Havel, H.A.1    Kauffman, E.W.2    Plaisted, S.M.3    Brems, D.N.4
  • 21
    • 0024503217 scopus 로고
    • Investigations of protein structure with optical spectroscopy: Bovine growth hormone
    • Havel, H. A., Chao, R. S., Haskell, R. J., Thamann, T. J. (1989) Investigations of protein structure with optical spectroscopy: bovine growth hormone. Anal. Chem. 61: 642-650
    • (1989) Anal. Chem. , vol.61 , pp. 642-650
    • Havel, H.A.1    Chao, R.S.2    Haskell, R.J.3    Thamann, T.J.4
  • 22
    • 0025847743 scopus 로고
    • Glycosaminoglycans: Molecular properties, protein interactions, and role in physiological processes
    • Jackson, R. L., Busch, S. J., Cardin, A. D. (1991) Glycosaminoglycans: molecular properties, protein interactions, and role in physiological processes. Physiol. Rev. 71: 481-539
    • (1991) Physiol. Rev. , vol.71 , pp. 481-539
    • Jackson, R.L.1    Busch, S.J.2    Cardin, A.D.3
  • 23
    • 0031391073 scopus 로고    scopus 로고
    • Use of poloxamer polymers to stabilize recombinant human growth hormone against various processing stresses
    • Katakam, M., Banga, A. K. (1997) Use of poloxamer polymers to stabilize recombinant human growth hormone against various processing stresses. Pharm. Dev. Technol. 2: 143-149
    • (1997) Pharm. Dev. Technol. , vol.2 , pp. 143-149
    • Katakam, M.1    Banga, A.K.2
  • 24
    • 0029074530 scopus 로고
    • Effect of surfactants on the physical stability of recombinant human growth hormone
    • Katakam, M., Bell, L., Banga, A. (1995) Effect of surfactants on the physical stability of recombinant human growth hormone. J. Pharm. Sci. 84: 713-716
    • (1995) J. Pharm. Sci. , vol.84 , pp. 713-716
    • Katakam, M.1    Bell, L.2    Banga, A.3
  • 25
    • 0030929076 scopus 로고    scopus 로고
    • Effects of growth hormone and low dose estrogen on bone growth and turnover in long bones of hypophysectomized rats
    • Kidder, L. S., Schmidt, I. U., Evans, G. L., Turner, R. T. (1997) Effects of growth hormone and low dose estrogen on bone growth and turnover in long bones of hypophysectomized rats. Calcif. Tissue Int. 61: 327-335
    • (1997) Calcif. Tissue Int. , vol.61 , pp. 327-335
    • Kidder, L.S.1    Schmidt, I.U.2    Evans, G.L.3    Turner, R.T.4
  • 26
    • 0030570127 scopus 로고    scopus 로고
    • Membrane fouling in sterile filtration of recombinant human growth hormone
    • Maa, Y. F., Hsu, C. C. (1996) Membrane fouling in sterile filtration of recombinant human growth hormone. Biotechriol. Bioeng. 50: 319-328
    • (1996) Biotechriol. Bioeng. , vol.50 , pp. 319-328
    • Maa, Y.F.1    Hsu, C.C.2
  • 28
    • 0024318970 scopus 로고
    • pH-dependence of the reversible and irreversible thermal-denaturation of gamma-interferons
    • Mulkerrini M. G., Wetzel, R. (1989) pH-dependence of the reversible and irreversible thermal-denaturation of gamma-interferons. Biochemistry 28: 6556-6561
    • (1989) Biochemistry , vol.28 , pp. 6556-6561
    • Mulkerrini, M.G.1    Wetzel, R.2
  • 29
    • 0027972452 scopus 로고
    • Feasibility study on spray-drying protein pharmaceuticals: Recombinant human growth hormone and tissue-type plasminogen activator
    • Mumunthaler, M., Hsu, C. C., Pearlman, R. (1994) Feasibility study on spray-drying protein pharmaceuticals: recombinant human growth hormone and tissue-type plasminogen activator. Pharm. Res. 11: 12-20
    • (1994) Pharm. Res. , vol.11 , pp. 12-20
    • Mumunthaler, M.1    Hsu, C.C.2    Pearlman, R.3
  • 31
    • 0021759419 scopus 로고
    • Determination of tyrosine exposure in proteins by second-derivative spectroscopy
    • Ragone, R., Colonna, G., Balestrieri, C, Servillo, L., Irace, G. (1984) Determination of tyrosine exposure in proteins by second-derivative spectroscopy. Biochemistry 23: 1871-1875
    • (1984) Biochemistry , vol.23 , pp. 1871-1875
    • Ragone, R.1    Colonna, G.2    Balestrieri, C.3    Servillo, L.4    Irace, G.5
  • 34
    • 84910894461 scopus 로고
    • The chemical physiology of mucopolysaccharides
    • Quintarelli, G. (ed.). Little, Brown, Boston
    • Scott, J. E. (1968) The chemical physiology of mucopolysaccharides. In: Quintarelli, G. (ed.) Ion binding in solutions containing acid mucopolysaccharides. Little, Brown, Boston, pp 171-187
    • (1968) Ion Binding in Solutions Containing Acid Mucopolysaccharides , pp. 171-187
    • Scott, J.E.1
  • 35
    • 85008072149 scopus 로고
    • Second derivative spectral properties of tryptophan and tyrosine residues in proteins. Effects of guanidine hydrochloride and dodecyl sulfate on the residues in lysozyme, ribonuclease and serum albumin
    • Terada, H., Inoue, Y., Ichikawa, T. (1984) Second derivative spectral properties of tryptophan and tyrosine residues in proteins. Effects of guanidine hydrochloride and dodecyl sulfate on the residues in lysozyme, ribonuclease and serum albumin. Chem. Pharm. Bull. 32: 585-590
    • (1984) Chem. Pharm. Bull. , vol.32 , pp. 585-590
    • Terada, H.1    Inoue, Y.2    Ichikawa, T.3
  • 36
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated
    • Timasheff, S. N. (1998) Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Adv. Protein Chem. 51: 355-432
    • (1998) Adv. Protein Chem. , vol.51 , pp. 355-432
    • Timasheff, S.N.1
  • 38
    • 0032486768 scopus 로고    scopus 로고
    • II. Electrostatic effect in the aggregation of heat-denatured RNase a and implications for protein additive design
    • Tsai, A. M., van Zanten, J. H., Betenbaugh, M. J. (1998) II. Electrostatic effect in the aggregation of heat-denatured RNase a and implications for protein additive design. Biotechnol. Bioeng, 59: 281-285
    • (1998) Biotechnol. Bioeng. , vol.59 , pp. 281-285
    • Tsai, A.M.1    Van Zanten, J.H.2    Betenbaugh, M.J.3
  • 39
    • 0030338236 scopus 로고    scopus 로고
    • The characterization, stabilization, and formulation of acidic fibroblast growth factor
    • Volkin, D. B., Middaugh, C. R. (1996) The characterization, stabilization, and formulation of acidic fibroblast growth factor. Pharm. Biotechnol. 9: 181-217
    • (1996) Pharm. Biotechnol. , vol.9 , pp. 181-217
    • Volkin, D.B.1    Middaugh, C.R.2
  • 40
    • 17644413882 scopus 로고    scopus 로고
    • Preparation and characterization of novel, glycosaminoglycan-complexed human growth hormone formulations for improved bioavailability
    • Indianapolis, IN. AAPS PharmSci
    • Zamiri, C., Dadey, E. J. (2000) Preparation and characterization of novel, glycosaminoglycan-complexed human growth hormone formulations for improved bioavailability. American Association of Pharmaceutical Scientists, Annual Meeting. Indianapolis, IN. AAPS PharmSci, pp 1221
    • (2000) American Association of Pharmaceutical Scientists, Annual Meeting , pp. 1221
    • Zamiri, C.1    Dadey, E.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.