메뉴 건너뛰기




Volumn 11, Issue 3, 2016, Pages 169-179

Determination of the composition and functional activity of the conjugates of colloidal gold and antibodies

Author keywords

Antibodies; Conjugates; Enzyme linked immunosorbent assay; Gold nanoparticles

Indexed keywords

ANTIBODY; ANTIBODY CONJUGATE; COLLOIDAL GOLD; GOLD NANOPARTICLE; HUMAN IMMUNOGLOBULIN;

EID: 84995483142     PISSN: None     EISSN: 13063057     Source Type: Journal    
DOI: 10.12973/ejac.2016.130a     Document Type: Article
Times cited : (8)

References (31)
  • 1
    • 85013795111 scopus 로고    scopus 로고
    • 2nd Edition, Academic Press: San Diego
    • Hermanson, G. T. (2008). Bioconjugate Techniques, 2nd Edition, Academic Press: San Diego, p 1202.
    • (2008) Bioconjugate Techniques , pp. 1202
    • Hermanson, G.T.1
  • 6
    • 79961166724 scopus 로고    scopus 로고
    • A review on functionalized gold nanoparticles for biosensing applications
    • Zeng, S., Yong, K. T., Roy, I., Dinh, X. Q., Yu, X. & Luan, F. (2011). A review on functionalized gold nanoparticles for biosensing applications. Plasmonics 6, 491.
    • (2011) Plasmonics , vol.6 , pp. 491
    • Zeng, S.1    Yong, K.T.2    Roy, I.3    Dinh, X.Q.4    Yu, X.5    Luan, F.6
  • 7
    • 79959259512 scopus 로고    scopus 로고
    • Analyzing nanomaterial bioconjugates: a review of current and emerging purification and characterization techniques
    • Sapsford, K. E., Tyner, K. M., Dair, B. J., Deschamps, J. R. & Medintz, I. L. (2011). Analyzing nanomaterial bioconjugates: a review of current and emerging purification and characterization techniques. Analytical Chemistry 83, 4453.
    • (2011) Analytical Chemistry , vol.83 , pp. 4453
    • Sapsford, K.E.1    Tyner, K.M.2    Dair, B.J.3    Deschamps, J.R.4    Medintz, I.L.5
  • 8
    • 84856734689 scopus 로고    scopus 로고
    • Influence of particle size on the binding activity of proteins adsorbed onto gold nanoparticles
    • Kaur, K. & Forrest, J. A. (2012). Influence of particle size on the binding activity of proteins adsorbed onto gold nanoparticles. Langmuir 28, 2736.
    • (2012) Langmuir , vol.28 , pp. 2736
    • Kaur, K.1    Forrest, J.A.2
  • 10
    • 84920190934 scopus 로고    scopus 로고
    • Development and application of a label-free fluorescence method for determining the composition of gold nanoparticle-protein conjugates
    • Sotnikov, D. V., Zherdev, A. V. & Dzantiev, B. B. (2014). Development and application of a label-free fluorescence method for determining the composition of gold nanoparticle-protein conjugates. International Journal of Molecular Sciences 16, 907.
    • (2014) International Journal of Molecular Sciences , vol.16 , pp. 907
    • Sotnikov, D.V.1    Zherdev, A.V.2    Dzantiev, B.B.3
  • 11
    • 84890260763 scopus 로고    scopus 로고
    • Multiplexed quantification of surface-bound proteins on gold nanoparticles
    • Hong, S. H., Kim, M., Ahn, J. H. & Yeo, W. S. (2013). Multiplexed quantification of surface-bound proteins on gold nanoparticles. Analytical Methods 5, 3816.
    • (2013) Analytical Methods , vol.5 , pp. 3816
    • Hong, S.H.1    Kim, M.2    Ahn, J.H.3    Yeo, W.S.4
  • 13
    • 84883209044 scopus 로고    scopus 로고
    • Quantitation of IgG protein adsorption to gold nanoparticles using particle size measurement
    • Bell, N. C., Minelli C. & Shard, A. G. (2013). Quantitation of IgG protein adsorption to gold nanoparticles using particle size measurement. Analytical Methods 5, 4591.
    • (2013) Analytical Methods , vol.5 , pp. 4591
    • Bell, N.C.1    Minelli, C.2    Shard, A.G.3
  • 16
    • 54549085780 scopus 로고    scopus 로고
    • Experimental determination of quantum dot size distributions, ligand packing densities, and bioconjugation using analytical ultracentrifugation
    • Lees, E. E., Gunzburg, M. J., Nguyen, T. L., Howlett, G. J., Rothacker, J., Nice, E. C., Clayton, A. H. A. & Mulvaney, P. (2008). Experimental determination of quantum dot size distributions, ligand packing densities, and bioconjugation using analytical ultracentrifugation. Nano Letters 8, 2883.
    • (2008) Nano Letters , vol.8 , pp. 2883
    • Lees, E.E.1    Gunzburg, M.J.2    Nguyen, T.L.3    Howlett, G.J.4    Rothacker, J.5    Nice, E.C.6    Clayton, A.H.A.7    Mulvaney, P.8
  • 17
    • 78049352573 scopus 로고    scopus 로고
    • Fractionation and characterization of gold nanoparticles in aqueous solution: asymmetric-flow field flow fractionation with MALS, DLS, and UV-Vis detection
    • Cho, T. J. & Hackley, V. A. (2010). Fractionation and characterization of gold nanoparticles in aqueous solution: asymmetric-flow field flow fractionation with MALS, DLS, and UV-Vis detection. Analytical & Bioanalytical Chemistry 398, 2003.
    • (2010) Analytical & Bioanalytical Chemistry , vol.398 , pp. 2003
    • Cho, T.J.1    Hackley, V.A.2
  • 19
    • 79952583790 scopus 로고    scopus 로고
    • Adsorption and conformation of serum albumin protein on gold nanoparticles investigated using dimensional measurements and in situ spectroscopic methods
    • Tsai, D. H., DelRio, F. W., Keene, A. M., Tyner, K. M., MacCuspie, R. I., Cho, T. J., Zachariah, M. R. & Hackley, V. A. (2011). Adsorption and conformation of serum albumin protein on gold nanoparticles investigated using dimensional measurements and in situ spectroscopic methods. Langmuir 27, 2464.
    • (2011) Langmuir , vol.27 , pp. 2464
    • Tsai, D.H.1    DelRio, F.W.2    Keene, A.M.3    Tyner, K.M.4    MacCuspie, R.I.5    Cho, T.J.6    Zachariah, M.R.7    Hackley, V.A.8
  • 20
    • 84862525746 scopus 로고    scopus 로고
    • In situ measurement of bovine serum albumin interaction with gold nanospheres
    • Dominguez-Medina, S., McDonough, S., Swanglap, P., Landes, C. F. & Link, S. (2012). In situ measurement of bovine serum albumin interaction with gold nanospheres. Langmuir 28, 9131.
    • (2012) Langmuir , vol.28 , pp. 9131
    • Dominguez-Medina, S.1    McDonough, S.2    Swanglap, P.3    Landes, C.F.4    Link, S.5
  • 22
    • 79959243546 scopus 로고    scopus 로고
    • Contrasting effect of gold nanoparticles and nanorods with different surface modifications on the structure and activity of bovine serum albumin
    • Chakraborty, S., Joshi, P., Shanker, V., Ansari, Z. A., Singh, S. P. & Chakrabarti, P. (2011). Contrasting effect of gold nanoparticles and nanorods with different surface modifications on the structure and activity of bovine serum albumin. Langmuir 27, 7722.
    • (2011) Langmuir , vol.27 , pp. 7722
    • Chakraborty, S.1    Joshi, P.2    Shanker, V.3    Ansari, Z.A.4    Singh, S.P.5    Chakrabarti, P.6
  • 23
    • 84862525746 scopus 로고    scopus 로고
    • In situ measurement of bovine serum albumin interaction with gold nanospheres
    • Dominguez-Medina, S., McDonough, S., Swanglap, P., Landes, C. F. & Link, S. (2012). In situ measurement of bovine serum albumin interaction with gold nanospheres. Langmuir 28, 9131.
    • (2012) Langmuir , vol.28 , pp. 9131
    • Dominguez-Medina, S.1    McDonough, S.2    Swanglap, P.3    Landes, C.F.4    Link, S.5
  • 25
    • 26444569477 scopus 로고    scopus 로고
    • Probing BSA binding to citrate-coated gold nanoparticles and surfaces
    • Brewer, S. H., Glomm, W. R., Johnson, M. C., Knag, M. K. & Franzen, S. (2005). Probing BSA binding to citrate-coated gold nanoparticles and surfaces. Langmuir 21, 9303.
    • (2005) Langmuir , vol.21 , pp. 9303
    • Brewer, S.H.1    Glomm, W.R.2    Johnson, M.C.3    Knag, M.K.4    Franzen, S.5
  • 26
    • 57249084197 scopus 로고    scopus 로고
    • Au nanoparticle-based surface energy transfer probe for conformational changes of BSA protein
    • Sen, T., Haldar, K. K. & Patra, A. (2008). Au nanoparticle-based surface energy transfer probe for conformational changes of BSA protein. The Journal of Physical Chemistry C 112, 17945.
    • (2008) The Journal of Physical Chemistry C , vol.112 , pp. 17945
    • Sen, T.1    Haldar, K.K.2    Patra, A.3
  • 27
    • 79955721224 scopus 로고    scopus 로고
    • Fluorescence manipulation by gold nanoparticles: from complete quenching to extensive enhancement
    • Kang, K. A., Wang, J., Jasinski, J. B. & Achilefu, S. (2011). Fluorescence manipulation by gold nanoparticles: from complete quenching to extensive enhancement. Journal of Nanobiotechnology 9, 16.
    • (2011) Journal of Nanobiotechnology , vol.9 , pp. 16
    • Kang, K.A.1    Wang, J.2    Jasinski, J.B.3    Achilefu, S.4
  • 28
    • 84867314505 scopus 로고    scopus 로고
    • Fluorescence quenching of gold nanoparticles integrating with a conformation-switched hairpin oligonucleotide probe for microRNA detection
    • Tu, Y., Wu, P., Zhang, H. & Cai, C. (2012). Fluorescence quenching of gold nanoparticles integrating with a conformation-switched hairpin oligonucleotide probe for microRNA detection. Chemical Communications 48, 10718.
    • (2012) Chemical Communications , vol.48 , pp. 10718
    • Tu, Y.1    Wu, P.2    Zhang, H.3    Cai, C.4
  • 29
    • 85052348446 scopus 로고
    • Controlled nucleation for the regulation of the particle size in monodisperse gold suspensio, Nature 241, 20. © 2016 iSER
    • Frens, G. (1973). Controlled nucleation for the regulation of the particle size in monodisperse gold suspensions. Nature 241, 20. © 2016 iSER, Eurasian J Anal Chem, 11(3), 169-179 179.
    • (1973) Eurasian J Anal Chem , vol.11 , Issue.3 , pp. 169-179
    • Frens, G.1
  • 30
    • 84861229666 scopus 로고    scopus 로고
    • Factors influencing the detection limit of the lateral-flow sandwich immunoassay: a case study with potato virus X
    • Safenkova, I., Zherdev, A. & Dzantiev, B. (2012). Factors influencing the detection limit of the lateral-flow sandwich immunoassay: a case study with potato virus X. Analytical & Bioanalytical Chemistry 403, 1595.
    • (2012) Analytical & Bioanalytical Chemistry , vol.403 , pp. 1595
    • Safenkova, I.1    Zherdev, A.2    Dzantiev, B.3
  • 31
    • 77949280649 scopus 로고    scopus 로고
    • Rapid pretreatment-free immunochromatographic assay of chloramphenicol in milk
    • Byzova, N. A., Zvereva, E. A., Zherdev, A. V., Eremin, S. A. & Dzantiev, B. B. (2010). Rapid pretreatment-free immunochromatographic assay of chloramphenicol in milk. Talanta 81, 843.
    • (2010) Talanta , vol.81 , pp. 843
    • Byzova, N.A.1    Zvereva, E.A.2    Zherdev, A.V.3    Eremin, S.A.4    Dzantiev, B.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.