메뉴 건너뛰기




Volumn 10, Issue 3, 1999, Pages 395-400

Temperature control of biotin binding and release with A streptavidin-poly(N-isopropylacrylamide) site-specific conjugate

Author keywords

[No Author keywords available]

Indexed keywords

ACRYLIC MONOMERS; AMIDES; AMINO ACIDS; BINDING ENERGY; COENZYMES; CONFORMATIONS; CONJUGATED POLYMERS; FREE ENERGY;

EID: 0033136648     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc980108s     Document Type: Article
Times cited : (110)

References (36)
  • 1
    • 0024588901 scopus 로고
    • Structural origins of high-affinity biotin binding to streptavidin
    • Weber, P. C., Ohlendore, D. H., Wendoloski, J. J., and Salemme, F. R. (1989) Structural origins of high-affinity biotin binding to streptavidin. Science 243, 85-8.
    • (1989) Science , vol.243 , pp. 85-88
    • Weber, P.C.1    Ohlendore, D.H.2    Wendoloski, J.J.3    Salemme, F.R.4
  • 2
    • 0031260274 scopus 로고    scopus 로고
    • Site-specific incorporation of biotinylated amino acids to identify surface-exposed residues in integral membrane proteins
    • Gallivan, J. P., Lester, H. A., and Dougherty, D. A. (1997) Site-specific incorporation of biotinylated amino acids to identify surface-exposed residues in integral membrane proteins. Chemistry Biol. 4, 739-49.
    • (1997) Chemistry Biol. , vol.4 , pp. 739-749
    • Gallivan, J.P.1    Lester, H.A.2    Dougherty, D.A.3
  • 3
    • 1842343078 scopus 로고
    • Rapid affinity-purification and biotinyl-ation of antibodies
    • Peranen, J. (1992) Rapid affinity-purification and biotinyl-ation of antibodies. Biotechniques 13, 546-9.
    • (1992) Biotechniques , vol.13 , pp. 546-549
    • Peranen, J.1
  • 4
    • 0030769914 scopus 로고    scopus 로고
    • A highly sensitive detection method for immunohistocheimstry using biotinylated tyramine
    • King, G., Payne, S., Walker, F., and Murray, G. I. (1997) A highly sensitive detection method for immunohistocheimstry using biotinylated tyramine. J. Pathol. 183, 237-41.
    • (1997) J. Pathol. , vol.183 , pp. 237-241
    • King, G.1    Payne, S.2    Walker, F.3    Murray, G.I.4
  • 5
    • 0028022535 scopus 로고
    • The use of biotinylated poly(ADP-ribose) for studies on poly(ADP-ribose)-protein interaction
    • Narendja, F. M., and Sauermann, G. (1994) The use of biotinylated poly(ADP-ribose) for studies on poly(ADP-ribose)-protein interaction. Anal. Biochem. 220, 415-9.
    • (1994) Anal. Biochem. , vol.220 , pp. 415-419
    • Narendja, F.M.1    Sauermann, G.2
  • 6
    • 0028398153 scopus 로고
    • Quantitative immunoblot detection of rare proteins in whole cell extracts using biotinstrepavidin reagents
    • Stevenson, B. R., Richards, C. L., Howarth, A. G., Maraj, V. A., and Hibbard, J. G. (1994) Quantitative immunoblot detection of rare proteins in whole cell extracts using biotinstrepavidin reagents. J. Exp. Zool. 268, 224-8.
    • (1994) J. Exp. Zool. , vol.268 , pp. 224-228
    • Stevenson, B.R.1    Richards, C.L.2    Howarth, A.G.3    Maraj, V.A.4    Hibbard, J.G.5
  • 7
    • 0029003693 scopus 로고
    • Biotin in vitro translation, nonradioactive detection of cell-free synthesized proteins
    • Hoeltke, H. J., Ettl, I., Strobel, E., Leying, H., Zimmermann, M., and Zimmermann, R. (1995) Biotin in vitro translation, nonradioactive detection of cell-free synthesized proteins. Biotechniques 18, 900-4, 906-7.
    • (1995) Biotechniques , vol.18 , pp. 900-904
    • Hoeltke, H.J.1    Ettl, I.2    Strobel, E.3    Leying, H.4    Zimmermann, M.5    Zimmermann, R.6
  • 9
  • 10
    • 0030763293 scopus 로고    scopus 로고
    • Timed ELISA: An alternative approach to quantitative enzyme-linked immunosorbent assay
    • Muller, R. (1997) Timed ELISA: An alternative approach to quantitative enzyme-linked immunosorbent assay. Biotechnol. Appl. Biochem. 26, 73-78.
    • (1997) Biotechnol. Appl. Biochem. , vol.26 , pp. 73-78
    • Muller, R.1
  • 11
    • 0030838224 scopus 로고    scopus 로고
    • Sensitive monoclonal antibody-based sandwich ELISA for determination of the diabetes-associated autoantigen glutamic acid decarboxylase GAD65
    • Schlosser, M., Hahmann, J., Ziegler, B., Augstein, P., and Ziegler, M. (1997) Sensitive monoclonal antibody-based sandwich ELISA for determination of the diabetes-associated autoantigen glutamic acid decarboxylase GAD65. J. Immunoassay 18, 289-307.
    • (1997) J. Immunoassay , vol.18 , pp. 289-307
    • Schlosser, M.1    Hahmann, J.2    Ziegler, B.3    Augstein, P.4    Ziegler, M.5
  • 12
    • 0030772851 scopus 로고    scopus 로고
    • Enhanced cytokine detection by a novel cell culture-based ELISA
    • Shankar, G., and Cohen, D. A. (1997) Enhanced cytokine detection by a novel cell culture-based ELISA. J. Immunoassay 18, 371-88.
    • (1997) J. Immunoassay , vol.18 , pp. 371-388
    • Shankar, G.1    Cohen, D.A.2
  • 13
    • 0030224318 scopus 로고    scopus 로고
    • Immobilization of streptavidin for immunosensors on nanostructured surfaces
    • Kossek, S., Padeste, C., and Tiefenauer, L. (1996) Immobilization of streptavidin for immunosensors on nanostructured surfaces. J. Mol. Recognit. 9, 485-7.
    • (1996) J. Mol. Recognit. , vol.9 , pp. 485-487
    • Kossek, S.1    Padeste, C.2    Tiefenauer, L.3
  • 14
    • 0000178199 scopus 로고    scopus 로고
    • Biotin tagging deletion analysis of domain limits involved in protein-macromolecular interactions. Mapping the tau binding domain of the DNA polymerase III alpha subunit
    • Kim, D. R., and McHenry, C. S. (1996) Biotin tagging deletion analysis of domain limits involved in protein-macromolecular interactions. Mapping the tau binding domain of the DNA polymerase III alpha subunit. J. Biol. Chem. 271, 20690-8.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20690-20698
    • Kim, D.R.1    McHenry, C.S.2
  • 15
    • 0030612876 scopus 로고    scopus 로고
    • Hybridization capture of microsatellites directly from genomic DNA
    • Refseth, U. H., Fangan, B. M., and Jakobsen, K. S. (1997) Hybridization capture of microsatellites directly from genomic DNA. Electrophoresis 18, 1519-23.
    • (1997) Electrophoresis , vol.18 , pp. 1519-1523
    • Refseth, U.H.1    Fangan, B.M.2    Jakobsen, K.S.3
  • 16
    • 0028138704 scopus 로고
    • Fully automated, nonradioactive solid-phase sequencing of genomic DNA obtained from PCR
    • Rolfs, A., and Weber, I. (1994) Fully automated, nonradioactive solid-phase sequencing of genomic DNA obtained from PCR. Biotechniques 17, 782-4.
    • (1994) Biotechniques , vol.17 , pp. 782-784
    • Rolfs, A.1    Weber, I.2
  • 17
    • 0028291526 scopus 로고
    • Sequence analysis of 16S rRNA from mycoplasmas by direct solid-phase DNA sequencing
    • Pettersson, B., Johansson, K. E., and Uhlen, M. (1994) Sequence analysis of 16S rRNA from mycoplasmas by direct solid-phase DNA sequencing. Appl. Environ. Microbiol. 60, 2456-61.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 2456-2461
    • Pettersson, B.1    Johansson, K.E.2    Uhlen, M.3
  • 18
    • 0028922434 scopus 로고
    • The functional effects of biotinylation of anti-angiotensin-converting enzyme monoclonal antibody in terms of targeting in vivo
    • Muzykantov, V. R., Gavriluk, V. D., Reinecke, A., Atochina, E. N., Kuo, A., Barnathan, E. S., and Fisher, A. B. (1995) The functional effects of biotinylation of anti-angiotensin-converting enzyme monoclonal antibody in terms of targeting in vivo. Anal. Biochem. 226, 279-87.
    • (1995) Anal. Biochem. , vol.226 , pp. 279-287
    • Muzykantov, V.R.1    Gavriluk, V.D.2    Reinecke, A.3    Atochina, E.N.4    Kuo, A.5    Barnathan, E.S.6    Fisher, A.B.7
  • 19
    • 0028275694 scopus 로고
    • Nonisotopic detection of mutations using a modified single-strand conformation polymorphism analysis
    • Weidner, J., Eigel, A., Horst, J., and Koehnlein, W. (1994) Nonisotopic detection of mutations using a modified single-strand conformation polymorphism analysis. Human Mutat. 4, 55-6.
    • (1994) Human Mutat. , vol.4 , pp. 55-56
    • Weidner, J.1    Eigel, A.2    Horst, J.3    Koehnlein, W.4
  • 21
    • 0029996541 scopus 로고    scopus 로고
    • Reversibility of biotin-binding by selective modification of tyrosine in avidin
    • Morag, E., Bayer, E. A., and Wilchek, M. (1996) Reversibility of biotin-binding by selective modification of tyrosine in avidin. Biochem. J. 316, 193-9.
    • (1996) Biochem. J. , vol.316 , pp. 193-199
    • Morag, E.1    Bayer, E.A.2    Wilchek, M.3
  • 22
    • 0030037606 scopus 로고    scopus 로고
    • Synthesis and purification of thermally sensitive oligomerenzyme conjugates of poly(N-isopropylacrylamide)-trypsin
    • Ding, Z. L., Chen, G. H., and Hoffman, A. S. (1996) Synthesis and purification of thermally sensitive oligomerenzyme conjugates of poly(N-isopropylacrylamide)-trypsin. Bioconjugate Chem. 7, 121-5.
    • (1996) Bioconjugate Chem. , vol.7 , pp. 121-125
    • Ding, Z.L.1    Chen, G.H.2    Hoffman, A.S.3
  • 23
    • 0032485209 scopus 로고    scopus 로고
    • Unusual properties of thermally sensitive oligomer-enzyme conjugates of poly(N-isopropylacrylamide)-trypsin
    • Ding, Z. L., Chen, G., and Hoffman, A. S. (1998) Unusual properties of thermally sensitive oligomer-enzyme conjugates of poly(N-isopropylacrylamide)-trypsin. J. Biomed. Mater. Res. 39, 498-505.
    • (1998) J. Biomed. Mater. Res. , vol.39 , pp. 498-505
    • Ding, Z.L.1    Chen, G.2    Hoffman, A.S.3
  • 24
    • 0028539339 scopus 로고
    • Temperature-responsive bioconjugates. 3. Antibody-poly (N-isopropylacrylamide) conjugates for temperature-modulated precipitations and affinity bioseparations
    • Takei, Y. G., Matsukata, M., Aoki, T., Sanui, K., Ogata, N., Kikuchi, A., Sakurai, Y., and Okano, T. (1994) Temperature-responsive bioconjugates. 3. Antibody-poly (N-isopropylacrylamide) conjugates for temperature-modulated precipitations and affinity bioseparations. Bioconjugate Chem. 5, 577-82.
    • (1994) Bioconjugate Chem. , vol.5 , pp. 577-582
    • Takei, Y.G.1    Matsukata, M.2    Aoki, T.3    Sanui, K.4    Ogata, N.5    Kikuchi, A.6    Sakurai, Y.7    Okano, T.8
  • 25
    • 0025646474 scopus 로고
    • Polymer-protein conjugates. II. Affinity precipitation of human IgG by poly-(N-isopropylacrylamide)-protein A conjugates
    • Chen, J. P., and Hoffman, A. S. (1990) Polymer-protein conjugates. II. Affinity precipitation of human IgG by poly-(N-isopropylacrylamide)-protein A conjugates. Biomaterials 11, 631-4.
    • (1990) Biomaterials , vol.11 , pp. 631-634
    • Chen, J.P.1    Hoffman, A.S.2
  • 26
    • 2842539808 scopus 로고
    • A novel immunoassay system and bioseparation process based on thermal phase separating polymers
    • Monji, N., and Hoffman, A. S. (1987) A novel immunoassay system and bioseparation process based on thermal phase separating polymers. Appl. Biochem. Biotechnol 14, 107-20.
    • (1987) Appl. Biochem. Biotechnol , vol.14 , pp. 107-120
    • Monji, N.1    Hoffman, A.S.2
  • 27
    • 0023038764 scopus 로고
    • Thermally reversible hydrogels: II. Delivery and selective removal of substances in aqueous solutions
    • Hoffman, A. S., Afrassiabi, A., and Dong, L. C. (1986) Thermally reversible hydrogels: II. Delivery and selective removal of substances in aqueous solutions. J. Controlled Rel. 4, 213-22.
    • (1986) J. Controlled Rel. , vol.4 , pp. 213-222
    • Hoffman, A.S.1    Afrassiabi, A.2    Dong, L.C.3
  • 28
    • 0028063017 scopus 로고
    • Positive thermosensitive pulsatile drug release using negative thermosensitive hydrogels
    • Yoshida, R., Kaneko, Y., Sakai, K, Okano, T., Sakurai, Y., Bae, Y. H., and Kim, S. W. (1994) Positive thermosensitive pulsatile drug release using negative thermosensitive hydrogels. J. Controlled Rel. 32, 97-102.
    • (1994) J. Controlled Rel. , vol.32 , pp. 97-102
    • Yoshida, R.1    Kaneko, Y.2    Sakai, K.3    Okano, T.4    Sakurai, Y.5    Bae, Y.H.6    Kim, S.W.7
  • 29
    • 0030135376 scopus 로고    scopus 로고
    • Preparation and characterization of poly(ethylene glycol) vinyl sulfone
    • Morpurgo, M., Veronese, F. M., Kachensky, D., and Harris, J. M. (1996) Preparation and characterization of poly(ethylene glycol) vinyl sulfone. Bioconjugate Chem. 7, 363-8.
    • (1996) Bioconjugate Chem. , vol.7 , pp. 363-368
    • Morpurgo, M.1    Veronese, F.M.2    Kachensky, D.3    Harris, J.M.4
  • 31
    • 0028910003 scopus 로고
    • Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: Contributions of tryptophan residues 79, 108, and 120
    • Chilkoti, A., Tan, P. H., and Stayton, P. S. (1995) Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: contributions of tryptophan residues 79, 108, and 120. Proc.Natl. Acad. Sci. U.S.A. 92, 1754-8.
    • (1995) Proc.Natl. Acad. Sci. U.S.A. , vol.92 , pp. 1754-1758
    • Chilkoti, A.1    Tan, P.H.2    Stayton, P.S.3
  • 32
    • 0028674870 scopus 로고
    • Preparation and characterization of biotinylated red blood cells
    • Magnani, M., Chiarantini, L., and Mancini, U. (1994) Preparation and characterization of biotinylated red blood cells. Biotechnol. Appl. Biochem. 20, 335-45.
    • (1994) Biotechnol. Appl. Biochem. , vol.20 , pp. 335-345
    • Magnani, M.1    Chiarantini, L.2    Mancini, U.3
  • 33
    • 0345065774 scopus 로고    scopus 로고
    • Unpublished data
    • Unpublished data.
  • 34
    • 0030011015 scopus 로고    scopus 로고
    • Binding of biotinylated DNA to streptavidin-coated polystyrene latex: Effects of chain length and particle size
    • Huang, S. C., Stump, M. D., Weiss, R., and Caldwell, K. D. (1996) Binding of biotinylated DNA to streptavidin-coated polystyrene latex: effects of chain length and particle size. Anal. Biochem. 237, 115-22.
    • (1996) Anal. Biochem. , vol.237 , pp. 115-122
    • Huang, S.C.1    Stump, M.D.2    Weiss, R.3    Caldwell, K.D.4
  • 35
    • 0000779088 scopus 로고
    • Thermodynamically stable globule state of a single poly(N-isopropylacrylamide) chain in water
    • Wu, C., and Zhou, S. (1995) Thermodynamically stable globule state of a single poly(N-isopropylacrylamide) chain in water. Macromolecules 28, 5388-90.
    • (1995) Macromolecules , vol.28 , pp. 5388-5390
    • Wu, C.1    Zhou, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.