메뉴 건너뛰기




Volumn 67, Issue 2-3, 2000, Pages 261-274

Correlation between drug release kinetics from proteineous matrices and protein folding: Elasticity and compressibility study

Author keywords

Compressibility; Elasticity; Protein folding; Proteineous matrices

Indexed keywords

BOVINE SERUM ALBUMIN; NAPROXEN; OVALBUMIN;

EID: 0034601172     PISSN: 01683659     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-3659(00)00211-X     Document Type: Article
Times cited : (13)

References (30)
  • 1
    • 0002754043 scopus 로고
    • Macromolecular and modeling aspects of swelling-controlled systems
    • T.J. Roseman, & S.Z. Mansdorf. New York: Marcell Dekker Inc
    • Korsmeyer R.W., Peppas N.A. Macromolecular and modeling aspects of swelling-controlled systems. Roseman T.J., Mansdorf S.Z. Controlled Release Delivery Systems. 1983;77-89 Marcell Dekker Inc, New York.
    • (1983) Controlled Release Delivery Systems , pp. 77-89
    • Korsmeyer, R.W.1    Peppas, N.A.2
  • 3
    • 0025140854 scopus 로고
    • Sustained release albumin microspheres containing antimicrobial drugs: Effects of preparation conditions on kinetics of drug release
    • Egbaria K., Friedman M. Sustained release albumin microspheres containing antimicrobial drugs: Effects of preparation conditions on kinetics of drug release. J. Control. Rel. 14:1979;79-94.
    • (1979) J. Control. Rel. , vol.14 , pp. 79-94
    • Egbaria, K.1    Friedman, M.2
  • 4
    • 0024549944 scopus 로고
    • Evaluation of drug delivery following the administration of magnetic albumin microspheres containing adriamicin to the rat
    • Gallo J.M., Gupta P.K., Hung C.T., Perrier D.G. Evaluation of drug delivery following the administration of magnetic albumin microspheres containing adriamicin to the rat. J. Pharm. Sci. 78:1989;190-194.
    • (1989) J. Pharm. Sci. , vol.78 , pp. 190-194
    • Gallo, J.M.1    Gupta, P.K.2    Hung, C.T.3    Perrier, D.G.4
  • 5
    • 0025258954 scopus 로고
    • Release and absorption characteristics of novel theophilline sustained-release formulations: In vitro-in vivo correlation
    • Hussein Z., Friedman M. Release and absorption characteristics of novel theophilline sustained-release formulations: in vitro-in vivo correlation. Pharm. Res. 7:1990;1167-1171.
    • (1990) Pharm. Res , vol.7 , pp. 1167-1171
    • Hussein, Z.1    Friedman, M.2
  • 8
    • 0024653050 scopus 로고
    • Circular dichroic study of conformational changes in albumin
    • Barta P.P., Sasa K., Ueki T., Takeda K. Circular dichroic study of conformational changes in albumin. J. Protein Chem. 8:1989;221-229.
    • (1989) J. Protein Chem. , vol.8 , pp. 221-229
    • Barta, P.P.1    Sasa, K.2    Ueki, T.3    Takeda, K.4
  • 10
    • 0018459006 scopus 로고
    • The conformational consequences of maleylation of amino groups in ovalbumin
    • Qasim M.A., Salahuddin A. The conformational consequences of maleylation of amino groups in ovalbumin. J. Biochem. Tokyo. 85:1979;1029-1035.
    • (1979) J. Biochem. Tokyo , vol.85 , pp. 1029-1035
    • Qasim, M.A.1    Salahuddin, A.2
  • 11
    • 0019005874 scopus 로고
    • Determination of protein secondary structure in solution by vacum ultraviolet circular dichroism
    • Brahms S., Brahms J. Determination of protein secondary structure in solution by vacum ultraviolet circular dichroism. J. Mol. Biol. 138:1980;149-178.
    • (1980) J. Mol. Biol. , vol.138 , pp. 149-178
    • Brahms, S.1    Brahms, J.2
  • 12
    • 0018504052 scopus 로고
    • Thermal gelation properties of methyl and hydroxypropyl methylcellulose
    • Sarkar N. Thermal gelation properties of methyl and hydroxypropyl methylcellulose. J. Appl. Poly. Sci. 24:1979;1073-1087.
    • (1979) J. Appl. Poly. Sci. , vol.24 , pp. 1073-1087
    • Sarkar, N.1
  • 13
    • 33751499115 scopus 로고
    • Thermal gelation of globular proteins: Influence of protein conformation on gel strength
    • Wang C.H., Damodaran S. Thermal gelation of globular proteins: Influence of protein conformation on gel strength. J. Agric. Food Sci. 39:1991;433-438.
    • (1991) J. Agric. Food Sci. , vol.39 , pp. 433-438
    • Wang, C.H.1    Damodaran, S.2
  • 14
    • 84985713724 scopus 로고
    • Relaxation contribution to protein compressibility from ultrasonic data
    • Sarvazyan A.P., Hemmes P. Relaxation contribution to protein compressibility from ultrasonic data. Biopolymers. 18:1979;3015-3024.
    • (1979) Biopolymers , vol.18 , pp. 3015-3024
    • Sarvazyan, A.P.1    Hemmes, P.2
  • 15
    • 0022687553 scopus 로고
    • Changes of cytochrome C globule compressibility during red-ox transition
    • Kharakoz D.P., Mkhitaryan A.G. Changes of cytochrome C globule compressibility during red-ox transition. Mol. Biol. 20:1986;396-406.
    • (1986) Mol. Biol. , vol.20 , pp. 396-406
    • Kharakoz, D.P.1    Mkhitaryan, A.G.2
  • 16
    • 0025855018 scopus 로고
    • Ultrasonic velocimetry of biological compounds
    • Sarvazyan A.P. Ultrasonic velocimetry of biological compounds. Annu. Rev. Biophys. Biophys. Chem. 20:1991;321-342.
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 321-342
    • Sarvazyan, A.P.1
  • 17
    • 0030787855 scopus 로고    scopus 로고
    • Partial volumes and compressibilities of extended polypeptide chains in aqueous solution: Additivity scheme and implication of protein unfolding at normal and high pressure
    • Kharakoz D.P. Partial volumes and compressibilities of extended polypeptide chains in aqueous solution: Additivity scheme and implication of protein unfolding at normal and high pressure. Biochemistry. 36:1997;10276-10285.
    • (1997) Biochemistry , vol.36 , pp. 10276-10285
    • Kharakoz, D.P.1
  • 18
    • 0030034601 scopus 로고    scopus 로고
    • Compressibility as a means to detect and characterize globular protein states
    • Chalikian T.V., Breslauer K.J. Compressibility as a means to detect and characterize globular protein states. Proc. Natl. Acad. Sci. USA. 93:1996;1012-1014.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1012-1014
    • Chalikian, T.V.1    Breslauer, K.J.2
  • 19
    • 0030028764 scopus 로고    scopus 로고
    • Glycerol decreases the volume and compressibility of protein interior
    • Priev A., Almagor A., Yedgar S., Gavish B. Glycerol decreases the volume and compressibility of protein interior. Biochemistry. 35:1996;2061-2066.
    • (1996) Biochemistry , vol.35 , pp. 2061-2066
    • Priev, A.1    Almagor, A.2    Yedgar, S.3    Gavish, B.4
  • 20
    • 0031890529 scopus 로고    scopus 로고
    • Reduction of protein and compressibility by macromolecular cosolvents: Dependence on the cosolvent molecular weight
    • Almagor A., Priev A., Barshtein G., Gavish B., Yedgar S. Reduction of protein and compressibility by macromolecular cosolvents: dependence on the cosolvent molecular weight. Biochim. Biophys. Acta. 1382:1998;151-156.
    • (1998) Biochim. Biophys. Acta , vol.1382 , pp. 151-156
    • Almagor, A.1    Priev, A.2    Barshtein, G.3    Gavish, B.4    Yedgar, S.5
  • 21
    • 0021195067 scopus 로고
    • Amino acid, peptide and protein volume in solution
    • Zamyatnin A.A. Amino acid, peptide and protein volume in solution. Annu. Rev. Biophys. Bioeng. 13:1984;145-165.
    • (1984) Annu. Rev. Biophys. Bioeng. , vol.13 , pp. 145-165
    • Zamyatnin, A.A.1
  • 23
    • 0037888836 scopus 로고
    • Compression testing of cylindrical samples with an Instron universal testing machine
    • P. Sherman. London: Academic Press
    • Olkku J.E., Sherman P. Compression testing of cylindrical samples with an Instron universal testing machine. Sherman P. Food Texture and Rheology. 1979;157-175 Academic Press, London.
    • (1979) Food Texture and Rheology , pp. 157-175
    • Olkku, J.E.1    Sherman, P.2
  • 24
    • 0344103144 scopus 로고
    • Volume properties of ordinary water
    • Kell G.S.J. Volume properties of ordinary water. Chem. Eng. Data. 20:1975;97-108.
    • (1975) Chem. Eng. Data. , vol.20 , pp. 97-108
    • Kell, G.S.J.1
  • 25
    • 0015700007 scopus 로고
    • Ultrasonic measurements with milliliter liquid samples in the 0.5-100 MHz range
    • Eggers F., Funk T. Ultrasonic measurements with milliliter liquid samples in the 0.5-100 MHz range. Rev. Sci. Instrum. 44:1973;969-977.
    • (1973) Rev. Sci. Instrum. , vol.44 , pp. 969-977
    • Eggers, F.1    Funk, T.2
  • 26
    • 0020936133 scopus 로고
    • Chemical and physical structure of polymers as carriers for controlled release of bioactive agents: A review
    • Langer R., Peppas N. Chemical and physical structure of polymers as carriers for controlled release of bioactive agents: A review. JMS - Rev. Macromol. Chem. Phys. C23:1983;61-126.
    • (1983) JMS - Rev. Macromol. Chem. Phys. , vol.23 , pp. 61-126
    • Langer, R.1    Peppas, N.2
  • 27
    • 0029133348 scopus 로고
    • Relation between adiabatic and pseudoadiabatic compressibility in ultrasonic velocimetry
    • Notling B. Relation between adiabatic and pseudoadiabatic compressibility in ultrasonic velocimetry. J. Theor. Biol. 175:1995;191-196.
    • (1995) J. Theor. Biol. , vol.175 , pp. 191-196
    • Notling, B.1
  • 28
    • 0343249787 scopus 로고
    • Bulk elastic properties of aqueous solutions of certain carbohydrates
    • Shilnikov G.V., Priev A., Ahmedov A. Bulk elastic properties of aqueous solutions of certain carbohydrates. Biofizika. 36:1991;276-280.
    • (1991) Biofizika , vol.36 , pp. 276-280
    • Shilnikov, G.V.1    Priev, A.2    Ahmedov, A.3
  • 29
    • 0030943939 scopus 로고    scopus 로고
    • Molten globule state of equine β-lactoglubin
    • Ikeguchi M., Kato S., Shimizu A., Sugai S. Molten globule state of equine β-lactoglubin. Proteins. 27:1997;567-575.
    • (1997) Proteins , vol.27 , pp. 567-575
    • Ikeguchi, M.1    Kato, S.2    Shimizu, A.3    Sugai, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.