메뉴 건너뛰기




Volumn 337, Issue 1-2, 2007, Pages 109-117

Study on the thermal stability of green fluorescent protein (GFP) in glucose parenteral formulations

Author keywords

Decimal reduction time (D value); Glucose; Green fluorescent protein (GFP); Large volume parenteral solutions; Thermal stability

Indexed keywords

ACETIC ACID; BIOLOGICAL MARKER; EDETIC ACID; GLUCOSE; GREEN FLUORESCENT PROTEIN; PHOSPHATE; WATER;

EID: 34249113112     PISSN: 03785173     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijpharm.2006.12.041     Document Type: Article
Times cited : (18)

References (32)
  • 1
    • 34249044548 scopus 로고    scopus 로고
    • ABRASP, 2006. Brazilian Association of Parenteral Solutions Manufacturers. Available: http://www.abrasp.org.br.
  • 2
    • 0031795085 scopus 로고    scopus 로고
    • Biological indicators for steam sterilization: characterization of a rapid biological indicator utilizing Bacillus strearothermophilus spore-associated alpha-glucosidase enzyme
    • Albert H., Davies D.J., Woodson L.P., and Soper C.J. Biological indicators for steam sterilization: characterization of a rapid biological indicator utilizing Bacillus strearothermophilus spore-associated alpha-glucosidase enzyme. J. Appl. Microbiol. 85 (1998) 865-874
    • (1998) J. Appl. Microbiol. , vol.85 , pp. 865-874
    • Albert, H.1    Davies, D.J.2    Woodson, L.P.3    Soper, C.J.4
  • 3
    • 34249008769 scopus 로고    scopus 로고
    • Anvisa (Brazilian Health Vigilance Office, Ministry of Health), 1997. Directive no. 500/1997. Technical Regulation of Large Volume Parenteral Solutions (LVPS).
  • 4
    • 34249111483 scopus 로고    scopus 로고
    • Aster Medical Products, 2006. Available: http://www.aster.com.br.
  • 5
    • 0018789680 scopus 로고
    • Increased thermal stability of proteins in the presence of sugars and polyols
    • Back J.F., Oakenfull D., and Smith M.B. Increased thermal stability of proteins in the presence of sugars and polyols. Biochemistry 18 (1979) 5191-5196
    • (1979) Biochemistry , vol.18 , pp. 5191-5196
    • Back, J.F.1    Oakenfull, D.2    Smith, M.B.3
  • 6
    • 0030265428 scopus 로고    scopus 로고
    • Ultra high pressure treatment of orange juice: a kinetic study on inactivation of pectin methyl esterase
    • Basak S., and Ramaswamy H.S. Ultra high pressure treatment of orange juice: a kinetic study on inactivation of pectin methyl esterase. Food Res. Int. 29 (1996) 601-607
    • (1996) Food Res. Int. , vol.29 , pp. 601-607
    • Basak, S.1    Ramaswamy, H.S.2
  • 7
    • 4344614677 scopus 로고    scopus 로고
    • Effects of naturally occurring osmolytes: on protein stability and solubility: issues important in protein crystallization
    • Bolen D.W. Effects of naturally occurring osmolytes: on protein stability and solubility: issues important in protein crystallization. Methods 34 (2004) 312-322
    • (2004) Methods , vol.34 , pp. 312-322
    • Bolen, D.W.1
  • 8
  • 10
    • 2442688313 scopus 로고    scopus 로고
    • Detection of molecular diversity in Bacillus atrophaeus by amplified fragment length polymorphism analysis
    • Burke S.A., Wright J.D., Robinson M.K., Bronk B.V., and Warren R.L. Detection of molecular diversity in Bacillus atrophaeus by amplified fragment length polymorphism analysis. Appl. Environ. Microbiol. 70 (2004) 2786-2790
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 2786-2790
    • Burke, S.A.1    Wright, J.D.2    Robinson, M.K.3    Bronk, B.V.4    Warren, R.L.5
  • 11
    • 13444283735 scopus 로고    scopus 로고
    • A kinetic study on pectinesterase inactivation during continuous pasteurization of orange juice
    • Collet L.S.F.C.A., Shigeoka D.S., Badolato G.G., and Tadini C.C. A kinetic study on pectinesterase inactivation during continuous pasteurization of orange juice. J. Food Eng. 69 (2005) 125-129
    • (2005) J. Food Eng. , vol.69 , pp. 125-129
    • Collet, L.S.F.C.A.1    Shigeoka, D.S.2    Badolato, G.G.3    Tadini, C.C.4
  • 12
    • 4344565219 scopus 로고    scopus 로고
    • Ions from the Hofmeister series and osmolytes: effects on proteins in solution and in the crystallization process
    • Collins K.D. Ions from the Hofmeister series and osmolytes: effects on proteins in solution and in the crystallization process. Methods 34 (2004) 300-311
    • (2004) Methods , vol.34 , pp. 300-311
    • Collins, K.D.1
  • 13
    • 20744441866 scopus 로고    scopus 로고
    • Study of lipoxygenase and peroxidase as blanching indicator enzymes in peas: change of enzyme activity, ascorbic acid and chlorophylls during frozen storage
    • Gökmen V., Bahçeci K.S., Serpen A., and Acar J. Study of lipoxygenase and peroxidase as blanching indicator enzymes in peas: change of enzyme activity, ascorbic acid and chlorophylls during frozen storage. Lebensm. Wiss. Technol. 38 (2005) 903-908
    • (2005) Lebensm. Wiss. Technol. , vol.38 , pp. 903-908
    • Gökmen, V.1    Bahçeci, K.S.2    Serpen, A.3    Acar, J.4
  • 14
    • 0032104464 scopus 로고    scopus 로고
    • Kinetics of growth characteristics of micro-organisms in dextrose infusion solutions
    • Hugbo P.G., Mendie U.E., and Nasipuri R.N. Kinetics of growth characteristics of micro-organisms in dextrose infusion solutions. Int. J. Pharm. 167 (1998) 1-6
    • (1998) Int. J. Pharm. , vol.167 , pp. 1-6
    • Hugbo, P.G.1    Mendie, U.E.2    Nasipuri, R.N.3
  • 15
    • 34249035517 scopus 로고    scopus 로고
    • International Organization for Standardization, ISO 11137, 2000. Sterilization of Health Care Products-Radiation. Part 1. Requirements for Development, Validation and Routine Control of a Sterilization Process for Medical Devices.
  • 16
    • 34249043907 scopus 로고    scopus 로고
    • International Organization for Standardization, ISO 11138-1, 2000. Sterilization of Health Care Products-Biological Indicators. Part 1. General Requirements.
  • 17
    • 0025070999 scopus 로고
    • Alkaline serine proteinase from Thermomonospora fusca YX. Stability to heat and denaturants
    • Kristjansson M.M., and Kinsella J.E. Alkaline serine proteinase from Thermomonospora fusca YX. Stability to heat and denaturants. Biochem. J. 270 (1990) 51-55
    • (1990) Biochem. J. , vol.270 , pp. 51-55
    • Kristjansson, M.M.1    Kinsella, J.E.2
  • 19
    • 33644881093 scopus 로고    scopus 로고
    • Predicting the thermal inactivation of bacteria in a solid matrix: simulation studies on the relative effects of microbial thermal resistance parameters and process conditions
    • Mackey B.M., Kelly A.F., Colvin J.A., Robbins P.T., and Fryer P.J. Predicting the thermal inactivation of bacteria in a solid matrix: simulation studies on the relative effects of microbial thermal resistance parameters and process conditions. Int. J. Food Microbiol. 107 (2006) 295-303
    • (2006) Int. J. Food Microbiol. , vol.107 , pp. 295-303
    • Mackey, B.M.1    Kelly, A.F.2    Colvin, J.A.3    Robbins, P.T.4    Fryer, P.J.5
  • 20
    • 0030265222 scopus 로고    scopus 로고
    • Thermal inactivation of lysozyme as influenced by pH, sucrose and sodium chloride and inactivation and preservative effect in beer
    • Makki F., and Durance T.D. Thermal inactivation of lysozyme as influenced by pH, sucrose and sodium chloride and inactivation and preservative effect in beer. Food Res. Int. 29 (1996) 635-645
    • (1996) Food Res. Int. , vol.29 , pp. 635-645
    • Makki, F.1    Durance, T.D.2
  • 22
    • 0035813504 scopus 로고    scopus 로고
    • Sugars protect native and apo yeast alcohol dehydrogenase against irreversible thermoinactivation
    • Miroliaei M., and Nemat-Gorgani M. Sugars protect native and apo yeast alcohol dehydrogenase against irreversible thermoinactivation. Enzyme Microb. Technol. 29 (2001) 554-559
    • (2001) Enzyme Microb. Technol. , vol.29 , pp. 554-559
    • Miroliaei, M.1    Nemat-Gorgani, M.2
  • 23
    • 3042829676 scopus 로고    scopus 로고
    • Selective permeation and organic extraction of recombinant green fluorescent protein (GFPuv) from Escherichia coli
    • Penna T.C.V., and Ishii M. Selective permeation and organic extraction of recombinant green fluorescent protein (GFPuv) from Escherichia coli. BMC Biotechnol. 24 (2002). http://www.biomedcentral.com/1472-6750/2/7/qc
    • (2002) BMC Biotechnol. , vol.24
    • Penna, T.C.V.1    Ishii, M.2
  • 24
    • 0036242556 scopus 로고    scopus 로고
    • The effect of composition of parenteral solution on the thermal resistance of Bacillus stearothermophilus and Bacillus subtilis spores
    • Penna T.C.V., Marques M., Machoshvili I.A., and Ishii M. The effect of composition of parenteral solution on the thermal resistance of Bacillus stearothermophilus and Bacillus subtilis spores. Appl. Biochem. Biotechnol. 98-100 (2002) 539-551
    • (2002) Appl. Biochem. Biotechnol. , vol.98-100 , pp. 539-551
    • Penna, T.C.V.1    Marques, M.2    Machoshvili, I.A.3    Ishii, M.4
  • 25
    • 11244308944 scopus 로고    scopus 로고
    • Evaluation of recombinant green fluorescent protein, under various culture conditions and purification with HiTrap hydrophobic interaction chromatography resins
    • Penna T.C.V., Ishii M., Pessoa Jr. A., Nascimento L.O., De Souza L.C., and Cholewa O. Evaluation of recombinant green fluorescent protein, under various culture conditions and purification with HiTrap hydrophobic interaction chromatography resins. Appl. Biochem. Biotechnol. 113-116 (2004) 453-468
    • (2004) Appl. Biochem. Biotechnol. , vol.113-116 , pp. 453-468
    • Penna, T.C.V.1    Ishii, M.2    Pessoa Jr., A.3    Nascimento, L.O.4    De Souza, L.C.5    Cholewa, O.6
  • 26
    • 19944387632 scopus 로고    scopus 로고
    • Expression of green fluorescent protein (GFP) in Escherichia coli DH5-a, under different growth conditions
    • Penna T.C.V., Ishii M., Cholewa O., and De Souza L.C. Expression of green fluorescent protein (GFP) in Escherichia coli DH5-a, under different growth conditions. Afr. J. Biotechnol. 3 (2004) 105-111
    • (2004) Afr. J. Biotechnol. , vol.3 , pp. 105-111
    • Penna, T.C.V.1    Ishii, M.2    Cholewa, O.3    De Souza, L.C.4
  • 27
    • 1242264025 scopus 로고    scopus 로고
    • Thermal characteristics of recombinant green fluorescent protein (GFPuv) extracted from Escherichia coli
    • Penna T.C.V., Ishii M., Cholewa O., and De Souza L.C. Thermal characteristics of recombinant green fluorescent protein (GFPuv) extracted from Escherichia coli. Lett. Appl. Microbiol. 38 (2004) 135-139
    • (2004) Lett. Appl. Microbiol. , vol.38 , pp. 135-139
    • Penna, T.C.V.1    Ishii, M.2    Cholewa, O.3    De Souza, L.C.4
  • 28
    • 18844449372 scopus 로고    scopus 로고
    • Stability of recombinant green fluorescent protein (GFPuv) in glucose solutions at different concentrations and pH values
    • Penna T.C.V., Ishii M., Kunimura J.S., and Cholewa O. Stability of recombinant green fluorescent protein (GFPuv) in glucose solutions at different concentrations and pH values. Appl. Biochem. Biotechnol. 121-124 (2005) 501-528
    • (2005) Appl. Biochem. Biotechnol. , vol.121-124 , pp. 501-528
    • Penna, T.C.V.1    Ishii, M.2    Kunimura, J.S.3    Cholewa, O.4
  • 29
    • 0036171956 scopus 로고    scopus 로고
    • Microbicidal efficacy of superheated steam. II. Studies involving E. faecium and spores of B. xerothermodurans and B. coagulans
    • Spicher G., Peters J., Nürnberg M., and Schwebke I. Microbicidal efficacy of superheated steam. II. Studies involving E. faecium and spores of B. xerothermodurans and B. coagulans. Int. J. Hyg. Environ. Health 204 (2002) 309-316
    • (2002) Int. J. Hyg. Environ. Health , vol.204 , pp. 309-316
    • Spicher, G.1    Peters, J.2    Nürnberg, M.3    Schwebke, I.4
  • 32
    • 34249112870 scopus 로고    scopus 로고
    • US Pharmacopoeia XXVIII, 2004. US Pharmacopeial Convention, Rockville, MD, pp. 2537-2540.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.