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Volumn 519, Issue , 2017, Pages 42-50

A novel method for immobilization of proteins via entrapment of magnetic nanoparticles through epoxy cross-linking

Author keywords

Entrapment; Epichlorohydrin; Epoxy cross linking; Immobilization; Magnetic nanoparticles

Indexed keywords

EPICHLOROHYDRIN; ESTERASE; HORSERADISH PEROXIDASE; IMMOBILIZED ENZYME; IMMOBILIZED PROTEIN; IMMUNOGLOBULIN G ANTIBODY; PROTEIN A; ULTRASMALL SUPERPARAMAGNETIC IRON OXIDE; CROSS LINKING REAGENT; MAGNETITE NANOPARTICLE;

EID: 85006013237     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2016.12.007     Document Type: Article
Times cited : (29)

References (31)
  • 1
    • 57249114931 scopus 로고    scopus 로고
    • Magnetic nanoparticles and biosciences
    • [1] Safarik, I., Safarikova, M., Magnetic nanoparticles and biosciences. Monatsh. Fur Chem. 133 (2002), 737–759.
    • (2002) Monatsh. Fur Chem. , vol.133 , pp. 737-759
    • Safarik, I.1    Safarikova, M.2
  • 2
    • 84906656213 scopus 로고    scopus 로고
    • Application of iron magnetic nanoparticles in protein immobilization
    • [2] Xu, J., Sun, J., Wang, Y., Sheng, J., Wang, F., Sun, M., Application of iron magnetic nanoparticles in protein immobilization. Molecules 19 (2014), 11465–11486.
    • (2014) Molecules , vol.19 , pp. 11465-11486
    • Xu, J.1    Sun, J.2    Wang, Y.3    Sheng, J.4    Wang, F.5    Sun, M.6
  • 3
    • 84961289695 scopus 로고    scopus 로고
    • Fundamentals and application of magnetic particles in cell isolation and enrichment
    • [3] Plouffe, B.D., Murthy, S.K., Lewis, L.H., Fundamentals and application of magnetic particles in cell isolation and enrichment. Rep. Prog. Phys., 78, 2015, 016601, 10.1088/0034-4885/78/1/016601.
    • (2015) Rep. Prog. Phys. , vol.78 , pp. 016601
    • Plouffe, B.D.1    Murthy, S.K.2    Lewis, L.H.3
  • 4
    • 0022339451 scopus 로고
    • Estimation of thyroxin, triiodothyronine, thyrotropin, free thyroxin, and triiodothyronine uptake by use of magnetic-particle solid phases
    • [4] Witherspoon, L.R., Shuler, S.E., Gilbert, S., Estimation of thyroxin, triiodothyronine, thyrotropin, free thyroxin, and triiodothyronine uptake by use of magnetic-particle solid phases. Clin. Chem. 31 (1985), 415–419.
    • (1985) Clin. Chem. , vol.31 , pp. 415-419
    • Witherspoon, L.R.1    Shuler, S.E.2    Gilbert, S.3
  • 5
    • 0001755686 scopus 로고    scopus 로고
    • New developments in particle-based immonoassays: introduction
    • [5] Bangs, L.B., New developments in particle-based immonoassays: introduction. Pure Appl. Chem. 68 (1996), 1873–1879.
    • (1996) Pure Appl. Chem. , vol.68 , pp. 1873-1879
    • Bangs, L.B.1
  • 6
    • 47249140441 scopus 로고    scopus 로고
    • Magnetic iron oxide nanoparticles: synthesis, stabilization, vectorization, physicochemical characterizations, and biological applications
    • [6] Laurent, S., Forge, D., Port, M., Roch, A., Robic, C., Elst, L.V., Muller, R.N., Magnetic iron oxide nanoparticles: synthesis, stabilization, vectorization, physicochemical characterizations, and biological applications. Chem. Rev. 108 (2008), 2064–2110.
    • (2008) Chem. Rev. , vol.108 , pp. 2064-2110
    • Laurent, S.1    Forge, D.2    Port, M.3    Roch, A.4    Robic, C.5    Elst, L.V.6    Muller, R.N.7
  • 7
    • 0033652083 scopus 로고    scopus 로고
    • Improvement of MRI probes to allow efficient detection of gene expression
    • [7] Hogemann, D., Josephson, L., Weissleder, R., Basilion, J.P., Improvement of MRI probes to allow efficient detection of gene expression. Bioconjugate Chem. 11 (2000), 941–946.
    • (2000) Bioconjugate Chem. , vol.11 , pp. 941-946
    • Hogemann, D.1    Josephson, L.2    Weissleder, R.3    Basilion, J.P.4
  • 8
    • 70349495287 scopus 로고    scopus 로고
    • Structural and magnetic properties of starch-coated magnetite nanoparticles
    • [8] Dung, T.T., Danh, T.M., Hoa, L.T.M., Chien, D.M., Duc, N.H., Structural and magnetic properties of starch-coated magnetite nanoparticles. J. Exp. Nanosci. 4 (2009), 259–267.
    • (2009) J. Exp. Nanosci. , vol.4 , pp. 259-267
    • Dung, T.T.1    Danh, T.M.2    Hoa, L.T.M.3    Chien, D.M.4    Duc, N.H.5
  • 9
    • 0025416120 scopus 로고
    • Selective HGMS of colloidal magnetite- binding cells from whole blood
    • [9] Lauva, M., Auzans, E., Levitsky, V., Plavins, J., Selective HGMS of colloidal magnetite- binding cells from whole blood. J. Magn. Magn. Mater 85 (1990), 295–298.
    • (1990) J. Magn. Magn. Mater , vol.85 , pp. 295-298
    • Lauva, M.1    Auzans, E.2    Levitsky, V.3    Plavins, J.4
  • 10
    • 0025418090 scopus 로고
    • Magnetic fluids as a possible drug carrier for thrombosis treatment
    • [10] Rusetski, A.N., Ruuge, E.K., Magnetic fluids as a possible drug carrier for thrombosis treatment. J. Magn. Magn. Mater 85 (1990), 299–302.
    • (1990) J. Magn. Magn. Mater , vol.85 , pp. 299-302
    • Rusetski, A.N.1    Ruuge, E.K.2
  • 13
    • 77950285075 scopus 로고    scopus 로고
    • Controlled release of water soluble antibiotics by carboxymethylcellulose- and gelatin-based hydrogels crosslinked with epichlorohydrin
    • [13] Buhus, G., Peptu, C., Popa, M., Desbrières, J., Controlled release of water soluble antibiotics by carboxymethylcellulose- and gelatin-based hydrogels crosslinked with epichlorohydrin. Cellul. Chem. Technol. 43 (2009), 141–151.
    • (2009) Cellul. Chem. Technol. , vol.43 , pp. 141-151
    • Buhus, G.1    Peptu, C.2    Popa, M.3    Desbrières, J.4
  • 14
    • 84937010801 scopus 로고    scopus 로고
    • Affinity purification of antibodies
    • [14] Hnasko, R.M., McGarvey, J.A., Affinity purification of antibodies. Methods Mol. Biol. 1318 (2015), 29–41.
    • (2015) Methods Mol. Biol. , vol.1318 , pp. 29-41
    • Hnasko, R.M.1    McGarvey, J.A.2
  • 15
    • 84864089013 scopus 로고    scopus 로고
    • Synthetic human monoclonal antibodies toward Staphylococcal enterotoxin B (SEB) protective against toxic shock syndrome
    • [15] Karauzum, H., Chen, G., Abaandou, L., Mahmoudieh, M., Boroun, A.R., Synthetic human monoclonal antibodies toward Staphylococcal enterotoxin B (SEB) protective against toxic shock syndrome. J. Biol. Chem. 287 (2012), 25203–25215.
    • (2012) J. Biol. Chem. , vol.287 , pp. 25203-25215
    • Karauzum, H.1    Chen, G.2    Abaandou, L.3    Mahmoudieh, M.4    Boroun, A.R.5
  • 16
    • 84874530761 scopus 로고    scopus 로고
    • Association of Luteinizing hormone receptor (LHR) mRNA with its binding protein leads to decapping and degradation of the mRNA in the p bodies
    • [16] Menon, B., Sinden, J., Menon, K.M.J., Association of Luteinizing hormone receptor (LHR) mRNA with its binding protein leads to decapping and degradation of the mRNA in the p bodies. Biochim. Biophys. Acta 1833 (2013), 1173–1179.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 1173-1179
    • Menon, B.1    Sinden, J.2    Menon, K.M.J.3
  • 17
    • 84938197811 scopus 로고    scopus 로고
    • Hypusination of eukaryotic initiation factor 5A via cAMP-PKA-ERK1/2 pathway is required for ligand-induced downregulation of LH receptor mRNA expression in the ovary
    • [17] Gulappa, T., Menon, B., Menon, K.M.J., Hypusination of eukaryotic initiation factor 5A via cAMP-PKA-ERK1/2 pathway is required for ligand-induced downregulation of LH receptor mRNA expression in the ovary. Mol. Cell. Endocrinol. 413 (2015), 90–95.
    • (2015) Mol. Cell. Endocrinol. , vol.413 , pp. 90-95
    • Gulappa, T.1    Menon, B.2    Menon, K.M.J.3
  • 18
    • 0029584413 scopus 로고    scopus 로고
    • Non-enzymic protein induced hydrolysis of p-nitrophenyl acyl esters in relation to lipase/esterase assays
    • [18] Ostdal, H., Andersen, H., Non-enzymic protein induced hydrolysis of p-nitrophenyl acyl esters in relation to lipase/esterase assays. Food Chem. 55 (1996), 55–61.
    • (1996) Food Chem. , vol.55 , pp. 55-61
    • Ostdal, H.1    Andersen, H.2
  • 19
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • [19] Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976), 248–254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 21
    • 82755161670 scopus 로고    scopus 로고
    • Bioseparations: principles and Techniques
    • seventh ed. PHI Learning Pvt. Ltd. New Delhi
    • [21] Sivasankar, B., Bioseparations: principles and Techniques. seventh ed., 2010, PHI Learning Pvt. Ltd., New Delhi.
    • (2010)
    • Sivasankar, B.1
  • 22
    • 80155214273 scopus 로고    scopus 로고
    • Engineering the multifunctional surface on magnetic nanoparticles for targeted biomedical applications: a chemical approach
    • [22] Yiu, H.H.P., Engineering the multifunctional surface on magnetic nanoparticles for targeted biomedical applications: a chemical approach. Nanomedicine 6 (2011), 1429–1446.
    • (2011) Nanomedicine , vol.6 , pp. 1429-1446
    • Yiu, H.H.P.1
  • 23
    • 0028057451 scopus 로고
    • Adsorption and desorption of natural organic matter on iron oxide: mechanisms and models
    • [23] Gu, B.H., Schmitt, J., Chen, Z.H., Liang, L.Y., McCarthy, J.F., Adsorption and desorption of natural organic matter on iron oxide: mechanisms and models. Environ. Sci. Technol. 28 (1994), 38–46.
    • (1994) Environ. Sci. Technol. , vol.28 , pp. 38-46
    • Gu, B.H.1    Schmitt, J.2    Chen, Z.H.3    Liang, L.Y.4    McCarthy, J.F.5
  • 24
    • 85006081323 scopus 로고    scopus 로고
    • Protein A Magnetic Beads
    • Accessed 22.November.16
    • [24] ThermoFisher Scientific, Pierce™, Protein A Magnetic Beads. 2016 Accessed 22.November.16 https://www.thermofisher.com/order/catalog/product/88845.
    • (2016)
    • ThermoFisher Scientific, Pierce™,1
  • 25
    • 85005993649 scopus 로고    scopus 로고
    • Protein A Magnetic Beads
    • Accessed 22.November.16
    • [25] New England Biolabs Inc, Protein A Magnetic Beads. 2016 Accessed 22.November.16 https://www.neb.com/products/s1425-protein-a-magnetic-beads.
    • (2016)
    • New England Biolabs Inc1
  • 26
    • 85005993646 scopus 로고    scopus 로고
    • Immunoprecipitation performance of SureBeads TM Protein A Magnetic beads vs. Protein A Agarose beads, (n.d.)
    • (Accessed 22 November 16)
    • [26] Fihman, G., Tyagi, A., Heitkamp, S., Shezifi, D., Immunoprecipitation performance of SureBeads TM Protein A Magnetic beads vs. Protein A Agarose beads, (n.d.). Bio-Rad Bull., 6594 Rev A, 2016 (Accessed 22 November 16) www.bio-rad.com/webroot/web/pdf/lsr/literature/Bulletin_6594.pdf.
    • (2016) Bio-Rad Bull. , vol.6594
    • Fihman, G.1    Tyagi, A.2    Heitkamp, S.3    Shezifi, D.4
  • 27
    • 84879095331 scopus 로고    scopus 로고
    • Preparation of well-dispersed gold/magnetite nanoparticles embedded on cellulose nanocrystals for efficient immobilization of papain enzyme
    • [27] Mahmoud, K.A., Lam, E., Hrapovic, S., Luong, J.H., Preparation of well-dispersed gold/magnetite nanoparticles embedded on cellulose nanocrystals for efficient immobilization of papain enzyme. ACS Appl. Mater. Interfaces 5 (2013), 4978–4985.
    • (2013) ACS Appl. Mater. Interfaces , vol.5 , pp. 4978-4985
    • Mahmoud, K.A.1    Lam, E.2    Hrapovic, S.3    Luong, J.H.4
  • 28
    • 84871136430 scopus 로고    scopus 로고
    • Immobilization of bacterial luciferase into poly(N-isopropylacrylamide) film for electrochemical control of a bioluminescence reaction
    • [28] Kawanami, Y., Yamasaki, S., Yamada, S., Takehara, K., Immobilization of bacterial luciferase into poly(N-isopropylacrylamide) film for electrochemical control of a bioluminescence reaction. Anal. Sci. 28 (2012), 1013–1015.
    • (2012) Anal. Sci. , vol.28 , pp. 1013-1015
    • Kawanami, Y.1    Yamasaki, S.2    Yamada, S.3    Takehara, K.4
  • 29
    • 27944454801 scopus 로고    scopus 로고
    • Combined physical and chemical immobilization of glucose oxidase in alginate microspheres improves stability of encapsulation and activity
    • [29] Zhu, H., Srivastava, R., Brown, J.Q., McShane, M.J., Combined physical and chemical immobilization of glucose oxidase in alginate microspheres improves stability of encapsulation and activity. Bioconjugate Chem. 16 (2005), 1451–1458.
    • (2005) Bioconjugate Chem. , vol.16 , pp. 1451-1458
    • Zhu, H.1    Srivastava, R.2    Brown, J.Q.3    McShane, M.J.4
  • 30
    • 82355169618 scopus 로고    scopus 로고
    • Recent advances and applications of immobilized enzyme technologies
    • [30] Khan, A.A., Alzohairy, M.A., Recent advances and applications of immobilized enzyme technologies. Res. J. Biol. Sci. 5 (2010), 565–575.
    • (2010) Res. J. Biol. Sci. , vol.5 , pp. 565-575
    • Khan, A.A.1    Alzohairy, M.A.2
  • 31
    • 84867941046 scopus 로고    scopus 로고
    • A spectroscopic investigation on the interaction of a magnetic ferrofluid with a model plasma protein: effect on the conformation and activity of the protein
    • [31] Paul, B.K., Bhattacharjee, K., Bose, S., Guchhait, N., A spectroscopic investigation on the interaction of a magnetic ferrofluid with a model plasma protein: effect on the conformation and activity of the protein. Phys. Chem. Chem. Phys. 14 (2012), 15482–15493.
    • (2012) Phys. Chem. Chem. Phys. , vol.14 , pp. 15482-15493
    • Paul, B.K.1    Bhattacharjee, K.2    Bose, S.3    Guchhait, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.