메뉴 건너뛰기




Volumn 12, Issue 3, 2011, Pages 602-608

Endotoxin removing method based on lipopolysaccharide binding protein and polyhydroxyalkanoate binding protein PhaP

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC PROTEINS; BINDING PROTEINS; BOVINE SERUM ALBUMINS; ENDOTOXIN REMOVAL; FUSION PROTEINS; GENES ENCODING; GRANULE-ASSOCIATED PROTEINS; HIGH EFFICIENCY; HYDROPHOBIC POLYMERS; LIPOPOLYSACCHARIDES; MODEL PROTEINS; NON-TOXICITY; OVALBUMINS; PH CHANGE; PICHIA PASTORIS; POLY-HYDROXYALKANOATE; POLYHYDROXYALKANOATES; POLYHYDROXYBUTYRATE; PROTEIN PURIFICATION; PROTEIN RECOVERY; PROTEIN SOLUTION;

EID: 79955458160     PISSN: 15257797     EISSN: 15264602     Source Type: Journal    
DOI: 10.1021/bm101230n     Document Type: Article
Times cited : (36)

References (46)
  • 1
    • 0035975868 scopus 로고    scopus 로고
    • Endotoxin removal by affinity sobents
    • Anspach, F. B. Endotoxin removal by affinity sobents. J. Biochem. Biophys. Meth. 2001, 49, 665-681.
    • (2001) J. Biochem. Biophys. Meth. , vol.49 , pp. 665-681
    • Anspach, F.B.1
  • 2
    • 0034043139 scopus 로고    scopus 로고
    • Membrane adsorbers for selective endotoxin removal from protein solutions
    • DOI 10.1016/S0032-9592(00)00132-1, PII S0032959200001321
    • Anspach, F. B.; Petsch, D. Membrane adsorbers for selective endotoxin removal from protein solutions. Process Biochem. 2000, 35, 1005-1012. (Pubitemid 30414544)
    • (2000) Process Biochemistry , vol.35 , Issue.9 , pp. 1005-1012
    • Anspach, F.B.1    Petsch, D.2
  • 4
    • 0037415015 scopus 로고    scopus 로고
    • Evaluation of Lipopolysaccharide aggregation by light scattering spectroscopy
    • DOI 10.1002/cbic.200390020
    • Santos, N. C.; Silva, A. C.; Castanho, M. A. R. B.; Martins-Silva, J.; Saldanha, C. Evaluation of lipopolysaccharide aggregation by light scattering spectroscopy. Chem. Biochem. 2003, 4, 96-100. (Pubitemid 36114216)
    • (2003) ChemBioChem , vol.4 , Issue.1 , pp. 96-100
    • Santos, N.C.1    Silva, A.C.2    Castanho, M.A.R.B.3    Martins-Silva, J.4    Saldanha, C.5
  • 5
    • 0030882663 scopus 로고    scopus 로고
    • Removal of endotoxin from recombinant protein preparations
    • DOI 10.1016/S0009-9120(97)00049-0, PII S0009912097000490
    • Liu, S.; Tobias, R.; McClure, S.; Styba, G.; Shi, Q.; Jackoweki, G. Removal of endotoxin from recombinant protein preparations. Clin. Biochem. 1997, 30, 455-463. (Pubitemid 27418541)
    • (1997) Clinical Biochemistry , vol.30 , Issue.6 , pp. 455-463
    • Liu, S.1    Tobias, R.2    McClure, S.3    Styba, G.4    Shi, Q.5    Jackowski, G.6
  • 7
    • 0033991321 scopus 로고    scopus 로고
    • Endotoxin removal from protein solutions
    • Petsch, D.; Anspach, F. B. Endotoxin removal from protein solutions. J. Biotechnol. 2000, 76, 97-119.
    • (2000) J. Biotechnol. , vol.76 , pp. 97-119
    • Petsch, D.1    Anspach, F.B.2
  • 8
    • 0035975903 scopus 로고    scopus 로고
    • Affinity membrane chromatography for the analysis and purification of proteins
    • Zou, H. F.; Luo, Q. Z.; Zhou, D. M. Affinity membrane chromatography for the analysis and purification of proteins. J. Biochem. Biophys. Meth. 2001, 49, 199-240.
    • (2001) J. Biochem. Biophys. Meth. , vol.49 , pp. 199-240
    • Zou, H.F.1    Luo, Q.Z.2    Zhou, D.M.3
  • 9
    • 34447274012 scopus 로고    scopus 로고
    • Synthesis of an affinity adsorbent based on silica gel and its application in endotoxin removal
    • DOI 10.1016/j.reactfunctpolym.2007.05.003, PII S1381514807000818
    • Zhang, Y. Y.; Yang, H.; Zhou, K.; Ping, Z. H. Synthesis of an affinity adsorbent based on silica gel and its application in endotoxin removal. React. Funct. Polym. 2007, 67, 728-736. (Pubitemid 47048947)
    • (2007) Reactive and Functional Polymers , vol.67 , Issue.8 , pp. 728-736
    • Zhang, Y.1    Yang, H.2    Zhou, K.3    Ping, Z.4
  • 10
    • 0037681802 scopus 로고    scopus 로고
    • Optimization of buffer conditions for the removal of endotoxins using Q-sepharose
    • Lee, S. H.; Kim, J. S.; Kim, C. W. Optimization of buffer conditions for the removal of endotoxins using Q-sepharose. Process Biochem. 2003, 38, 1091-1098.
    • (2003) Process Biochem. , vol.38 , pp. 1091-1098
    • Lee, S.H.1    Kim, J.S.2    Kim, C.W.3
  • 12
    • 0032457308 scopus 로고    scopus 로고
    • Selective adsorption of endotoxin inside a polycationic network of flat-sheet microfiltration membranes
    • Petsch, D.; Rantze, E.; Anspach, F. B. Selective adsorption of endotoxin inside a polycationic network of flat-sheet microfiltration membranes. J. Mol. Recognit. 1998, 11, 22-230.
    • (1998) J. Mol. Recognit. , vol.11 , pp. 22-230
    • Petsch, D.1    Rantze, E.2    Anspach, F.B.3
  • 13
    • 58149386191 scopus 로고    scopus 로고
    • Selective assay for endotoxin using poly(e-lysine)-immobilized Cellufine and Limulus amoebocyte lysate
    • Sakata, M.; Fukuma, Y.; Todokoro, M.; Kunitake, M. Selective assay for endotoxin using poly(e-lysine)-immobilized Cellufine and Limulus amoebocyte lysate. Anal. Biochem. 2009, 385, 368-370.
    • (2009) Anal. Biochem. , vol.385 , pp. 368-370
    • Sakata, M.1    Fukuma, Y.2    Todokoro, M.3    Kunitake, M.4
  • 15
  • 16
    • 0031298184 scopus 로고    scopus 로고
    • Interchangeable Endotoxin-Binding Domains in Proteins with Opposite Lipopolysaccharide-Dependent Activities
    • Schumann, R. R.; Lamping, N.; Hoess, A. Interchangeable endotoxin-binding domains in proteins with opposite lipopolysaccharidedependent activities. J. Immunol. 1997, 159, 5599-5605. (Pubitemid 127470090)
    • (1997) Journal of Immunology , vol.159 , Issue.11 , pp. 5599-5605
    • Schumann, R.R.1    Lamping, N.2    Hoess, A.3
  • 17
    • 77953547610 scopus 로고    scopus 로고
    • Limulus amebocyte lysate assay for endotoxins by an adsorption method with polycation-immobilized cellulose beads
    • Sakata, M.; Inoue, T.; Todokoro, M.; kunitake, M. Limulus amebocyte lysate assay for endotoxins by an adsorption method with polycation-immobilized cellulose beads. Anal. Chem. 2010, 26, 291-297.
    • (2010) Anal. Chem. , vol.26 , pp. 291-297
    • Sakata, M.1    Inoue, T.2    Todokoro, M.3    Kunitake, M.4
  • 18
    • 10844287952 scopus 로고    scopus 로고
    • The functional and structural properties of MD-2 required for lipopolysaccharide binding are absent in MD-1
    • Tsuneyoshi, N.; Fukudome, K.; Kohara, J.; Tomimasu, R.; Gauchat, J. F.; Nakatake, H.; Kimoto, M. The functional and structural properties of MD-2 required for lipopolysaccharide binding are absent in MD-1. J. Immunol. 2005, 174, 340-344. (Pubitemid 40007421)
    • (2005) Journal of Immunology , vol.174 , Issue.1 , pp. 340-344
    • Tsuneyoshi, N.1    Fukudome, K.2    Kohara, J.3    Tomimasu, R.4    Gauchat, J.-F.5    Nakatake, H.6    Kimoto, M.7
  • 20
    • 33750327329 scopus 로고    scopus 로고
    • Induction of long-term lipopolysaccharide tolerance by an agonistic monoclonal antibody to the toll-like receptor 4/MD-2 complex
    • DOI 10.1128/CVI.00173-06
    • Ohta, S.; Bahrun, U.; Shimazu, R.; Matsushita, H.; Fukudome, K.; Kimoto, M. Induction of long-term lipopolysaccharide tolerance by an agonistic monoclonal antibody to the toll-like receptor 4/MD-2 complex. Clin. Vaccine Immunol. 2006, 10, 1131-1136. (Pubitemid 44622541)
    • (2006) Clinical and Vaccine Immunology , vol.13 , Issue.10 , pp. 1131-1136
    • Ohta, S.1    Bahrun, U.2    Shimazu, R.3    Matsushita, H.4    Fukudome, K.5    Kimoto, M.6
  • 22
    • 33646336635 scopus 로고    scopus 로고
    • Localization of the lipopolysaccharide-binding protein in phospholipid membranes by atomic force microscopy
    • DOI 10.1074/jbc.M507634200
    • Roes, S.; Mumm, F.; Seydel, U.; Gutsmann, T. Localization of the lipopolysaccharide-binding protein in phospholipid membranes by atomic force microscopy. J. Biol. Chem. 2006, 281, 2757-2763. (Pubitemid 43845739)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.5 , pp. 2757-2763
    • Roes, S.1    Mumm, F.2    Seydel, U.3    Gutsmann, T.4
  • 23
    • 0029028016 scopus 로고
    • Lipopolysaccharide (LPS) neutralizing peptides reveal a lipid A binding site of LPS binding protein
    • Taylor, H.; Heavner, G.; Nedelman, M.; Sherris, D.; Brunt, E.; Knight, D.; Ghrayeb, J. Lipopolysaccharide (LPS) neutralizing peptides reveal a lipid A binding site of LPS binding protein. J. Biol. Chem. 1995, 270, 17934-17938.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17934-17938
    • Taylor, H.1    Heavner, G.2    Nedelman, M.3    Sherris, D.4    Brunt, E.5    Knight, D.6    Ghrayeb, J.7
  • 24
    • 0035034359 scopus 로고    scopus 로고
    • Interaction between lipopolysaccharide (LPS), LPS-binding protein (LBP), and planar membranes
    • DOI 10.1515/BC.2001.052
    • Gutsmann, T.; Haberer, N.; Seydel, U.; Wiese, A. Interaction between lipopolysaccharide (LPS), LPS-binding protein (LBP), and planar membranes. Biol. Chem. 2001, 382, 425-434. (Pubitemid 32372486)
    • (2001) Biological Chemistry , vol.382 , Issue.3 , pp. 425-434
    • Gutsmann, T.1    Haberer, N.2    Carroll, S.F.3    Seydel, U.4    Wiese, A.5
  • 26
    • 0037415015 scopus 로고    scopus 로고
    • Evaluation of Lipopolysaccharide aggregation by light scattering spectroscopy
    • DOI 10.1002/cbic.200390020
    • Santos, N. C.; Silva, A. C.; Castanho, M. A. R. B.; Silva, J. M.; Saldanha, C. Evaluation of lipopolysaccharide aggregation by light scattering spectroscopy. ChemBioChem 2003, 4, 96-100. (Pubitemid 36114216)
    • (2003) ChemBioChem , vol.4 , Issue.1 , pp. 96-100
    • Santos, N.C.1    Silva, A.C.2    Castanho, M.A.R.B.3    Martins-Silva, J.4    Saldanha, C.5
  • 27
    • 0033802118 scopus 로고    scopus 로고
    • Polymer production by two newly isolated extremely Halophilic archaea: Application of a novel corrosion-resistant bioreactor
    • Hezayen, F. F.; Rehm, B. H. A.; Eberhardt, R.; Steinbüchel, A. Polymer production by two newly isolated extremely Halophilic archaea: application of a novel corrosion-resistant bioreactor. Appl. Microbiol. Biotechnol. 2000, 54, 319-325.
    • (2000) Appl. Microbiol. Biotechnol. , vol.54 , pp. 319-325
    • Hezayen, F.F.1    Rehm, B.H.A.2    Eberhardt, R.3    Steinbüchel, A.4
  • 28
    • 3242755883 scopus 로고    scopus 로고
    • Regulation of polyhydroxyalkanoate biosynthesis in Pseudomonas putida and Pseudomonas aeruginosa
    • DOI 10.1016/j.femsle.2004.06.029, PII S0378109704004483
    • Hoffmann, N.; Rehm, B. H. A. Regulation of polyhydroxyalkanoate biosynthesis in Pseudomonas putida and Pseudomonas aeruginosa. FEMS Microbiol. Lett. 2004, 237, 1-7. (Pubitemid 38979998)
    • (2004) FEMS Microbiology Letters , vol.237 , Issue.1 , pp. 1-7
    • Hoffmann, N.1    Rehm, B.H.A.2
  • 29
    • 33644961915 scopus 로고    scopus 로고
    • In vivo enzyme immobilization by use of engineered polyhydroxyalkanoate synthase
    • Peters, V.; Rehm, B. H. A. In vivo enzyme immobilization by use of engineered polyhydroxyalkanoate synthase. Appl. Environ. Microbiol. 2006, 72, 1777-1783.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 1777-1783
    • Peters, V.1    Rehm, B.H.A.2
  • 30
    • 6444241117 scopus 로고    scopus 로고
    • The role of polyhydroxyalkanoate biosynthesis by Pseudomonas aeruginosa in rhamnolipid and alginate production as well as stress tolerance and biofilm formation
    • DOI 10.1099/mic.0.27357-0
    • Pham, T. H.; Webb, J. S.; Rehm, B. H. A. The role of polyhydroxyalkanoate biosynthesis by Pseudomonas aeruginosa in rhamnolipid and alginate production as well as stress tolerance and biofilm formation. Microbiology 2004, 150, 3405-3413. (Pubitemid 39406209)
    • (2004) Microbiology , vol.150 , Issue.10 , pp. 3405-3413
    • Pham, T.H.1    Webb, J.S.2    Rehm, B.H.A.3
  • 31
    • 0345688125 scopus 로고    scopus 로고
    • Polyester synthases: Natural catalysts for plastics
    • DOI 10.1042/BJ20031254
    • Rehm, B. H. A. Polyester synthases: natural catalysts for plastics. Biochem. J. 2003, 376, 15-33. (Pubitemid 37487200)
    • (2003) Biochemical Journal , vol.376 , Issue.1 , pp. 15-33
    • Rehm, B.H.A.1
  • 32
    • 0035218357 scopus 로고    scopus 로고
    • Polyhydroxybutyrate biosynthesis in Caulobacter crescentus: Molecular characterization of the polyhydroxybutyrate synthase
    • Qi, Q.; Rehm, B. H. A. Polyhydroxybutyrate biosynthesis in Caulobacter crescentus: molecular characterization of the polyhydroxybutyrate synthase. Microbiology 2001, 147, 3353-3358. (Pubitemid 33150341)
    • (2001) Microbiology , vol.147 , Issue.12 , pp. 3353-3358
    • Qi, Q.1    Rehm, B.H.A.2
  • 33
    • 33846684899 scopus 로고    scopus 로고
    • Increased diversification of polyhydroxyalkanoates by modification reactions for industrial and medical applications
    • DOI 10.1007/s00253-006-0732-8
    • Hazer, B.; Steinbüchel, A. Increased diversification of polyhydroxyalkanoates by modification reactions for industrial and medical applications. Appl. Microbiol. Biotechnol. 2007, 74, 1-12. (Pubitemid 46188216)
    • (2007) Applied Microbiology and Biotechnology , vol.74 , Issue.1 , pp. 1-12
    • Hazer, B.1    Steinbuchel, A.2
  • 34
    • 24644468575 scopus 로고    scopus 로고
    • Selective immobilization of fusion proteins on poly(hydroxyalkanoate) microbeads
    • DOI 10.1021/ac0505223
    • Lee, S. J.; Park, J. P.; Park, T. J.; Lee, S. Y.; Lee, S.; Park, J. K. Selective immobilization of fusion proteins on poly(hydroxyalkanoate) microbeads. Anal. Chem. 2005, 77, 5755-5759. (Pubitemid 41266075)
    • (2005) Analytical Chemistry , vol.77 , Issue.17 , pp. 5755-5759
    • Lee, S.J.1    Park, J.P.2    Park, T.J.3    Lee, S.Y.4    Lee, S.5    Park, J.K.6
  • 35
    • 33845872800 scopus 로고    scopus 로고
    • Biomedical applications of polyhydroxyalkanoates, an overview of animal testing and in vivo responses
    • DOI 10.1586/17434440.3.6.853
    • Valappil, S. P.; Misra, S. K.; Boccaccini, A. R.; Roy, I. Biomedical applications of polyhydroxyalkanoates: an overview of animal testing and in vivo responses. Expert Rev. Med. Dev. 2006, 3, 853-868. (Pubitemid 46017624)
    • (2006) Expert Review of Medical Devices , vol.3 , Issue.6 , pp. 853-868
    • Valappil, S.P.1    Misra, S.K.2    Boccaccini, A.3    Roy, I.4
  • 36
    • 0029039870 scopus 로고
    • Analysis of a 24-kilodalton protein associated with the polyhydroxyalkanoic acid nanoparticles in Alcaligenes eutrophus
    • Wieczorek, R.; Pries, A.; Steinbüchel, A.;Mayer, F. Analysis of a 24-kilodalton protein associated with the polyhydroxyalkanoic acid nanoparticles in Alcaligenes eutrophus. J. Bacteriol. 1995, 177, 2425-2435.
    • (1995) J. Bacteriol. , vol.177 , pp. 2425-2435
    • Wieczorek, R.1    Pries, A.2    Steinbüchel, A.3    Mayer, F.4
  • 37
    • 0036667428 scopus 로고    scopus 로고
    • Regulation of phasin expression and polyhydroxyalkanoate (PHA) granule formation in Ralstonia eutropha H16
    • Potter, M.; Madkour, M. H.; Mayer, F.; Steinbüchel, A. Regulation of phasin expression and polyhydroxyalkanoate (PHA) granule formation in Ralstonia eutropha H16. Microbiology 2002, 148, 2413-2426.
    • (2002) Microbiology , vol.148 , pp. 2413-2426
    • Potter, M.1    Madkour, M.H.2    Mayer, F.3    Steinbüchel, A.4
  • 38
    • 33846807429 scopus 로고    scopus 로고
    • Recombinant Escherichia coli produces tailor-made biopolyester nanoparticles for applications in fluorescence activated cell sorting: Functional display of the mouse interleukin-2 and myelin oligodendrocyte glycoprotein
    • Bäckström, B. T.; Brockelbank, J. A.; Rehm, B. H. A. Recombinant Escherichia coli produces tailor-made biopolyester nanoparticles for applications in fluorescence activated cell sorting: functional display of the mouse interleukin-2 and myelin oligodendrocyte glycoprotein. BMC Biotechnol. 2007, 7, 3-15.
    • (2007) BMC Biotechnol. , vol.7 , pp. 3-15
    • Bäckström, B.T.1    Brockelbank, J.A.2    Rehm, B.H.A.3
  • 39
    • 54349115910 scopus 로고    scopus 로고
    • A novel self-cleaving phasing tag for purification of recombinant proteins based on hydrophobic polyhydroxyalkanoate nanoparticles
    • Wang, Z.; Wu, H.; Chen, J.; Zhang, J; Yao, Y.; Chen, G. Q. A novel self-cleaving phasing tag for purification of recombinant proteins based on hydrophobic polyhydroxyalkanoate nanoparticles. Lab Chip 2008, 8, 1957-1962.
    • (2008) Lab Chip , vol.8 , pp. 1957-1962
    • Wang, Z.1    Wu, H.2    Chen, J.3    Zhang, J.4    Yao, Y.5    Chen, G.Q.6
  • 40
    • 53449083912 scopus 로고    scopus 로고
    • A specific drug targeting system based on polyhydroxyalkanoate granule binding protein PhaP fused with targeted cell ligands
    • Yao, Y. C.; Zhan, X. Y.; Zhang, J.; Zou, X. H.; Wang, Z. H.; Xiong, Y. C.; Chen, G. Q. A specific drug targeting system based on polyhydroxyalkanoate granule binding protein PhaP fused with targeted cell ligands. Biomaterials 2008, 29, 4823-4830.
    • (2008) Biomaterials , vol.29 , pp. 4823-4830
    • Yao, Y.C.1    Zhan, X.Y.2    Zhang, J.3    Zou, X.H.4    Wang, Z.H.5    Xiong, Y.C.6    Chen, G.Q.7
  • 41
    • 0028766335 scopus 로고
    • Amorphous. biomimetic nanoparticles of polyhydroxybutyrate preparation, characterization, and biological implications
    • Horowitz, D. M.; Sanders, J. K. M. Amorphous, biomimetic nanoparticles of polyhydroxybutyrate preparation, characterization, and biological implications. J. Am. Chem. Soc. 1994, 116, 2695-2702.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 2695-2702
    • Horowitz, D.M.1    Sanders, J.K.M.2
  • 42
    • 58249086918 scopus 로고    scopus 로고
    • The effect of 3-hydroxybutyrate methyl ester on learning and memory in mice
    • Zou, X. H.; Chen, G. Q. The effect of 3-hydroxybutyrate methyl ester on learning and memory in mice. Biomaterials 2009, 30, 1532-1541.
    • (2009) Biomaterials , vol.30 , pp. 1532-1541
    • Zou, X.H.1    Chen, G.Q.2
  • 43
    • 33748776819 scopus 로고    scopus 로고
    • Preparation and characterization of truncated human lipopolysaccharide- binding protein in Escherichia coli
    • DOI 10.1016/j.pep.2006.05.015, PII S1046592806001677
    • Kohara, J.; Naoko, T. S.; Gauchat, J. F.; Kimoto, M.; Fukudome, K. J. Preparation and characterization of truncated human lipopolysaccharide- binding protein in Escherichia coli. Protein Exp. Purif. 2006, 49, 276-283. (Pubitemid 44416233)
    • (2006) Protein Expression and Purification , vol.49 , Issue.2 , pp. 276-283
    • Kohara, J.1    Tsuneyoshi, N.2    Gauchat, J.-F.3    Kimoto, M.4    Fukudome, K.5
  • 45
    • 0035882755 scopus 로고    scopus 로고
    • High-performance affinity capture-removal of bacterial pyrogen from solutions
    • DOI 10.1016/S0378-4347(01)00227-4, PII S0378434701002274
    • Ding, J. L.; Zhu, Y.; Ho, B. High-performance affinity captureremoval of bacterial pyrogen from solutions. J. Chromatogr., B 2001, 759, 237-246. (Pubitemid 32575284)
    • (2001) Journal of Chromatography B: Biomedical Sciences and Applications , vol.759 , Issue.2 , pp. 237-246
    • Ding, J.L.1    Zhu, Y.2    Ho, B.3
  • 46
    • 0023218429 scopus 로고
    • Induction of human interleukin-1 production by polymyxin B
    • DOI 10.1016/0022-1759(87)90215-8
    • Damais, C.; Jupin, C.; Parant, M.; Chedid, L. Induction of human interleukin-1 production by polymyxin B. J. Immunol. Methods 1987, 101, 51-56. (Pubitemid 17097897)
    • (1987) Journal of Immunological Methods , vol.101 , Issue.1 , pp. 51-56
    • Damais, C.1    Jupin, C.2    Parant, M.3    Chedid, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.