메뉴 건너뛰기




Volumn 38, Issue 4, 2009, Pages 407-414

Enzyme solid-state support assays: A surface plasmon resonance and mass spectrometry coupled study of immobilized insulin degrading enzyme

Author keywords

Conformational change; Insulin degrading enzyme; Mass spectrometry; Solid state assay; Surface plasmon resonance

Indexed keywords

ANIMALS; ATMOSPHERIC PRESSURE; CATTLE; ENZYMES, IMMOBILIZED; GOLD; INSULIN; INSULYSIN; KINETICS; MASS SPECTROMETRY; MICROFLUIDICS; PROTEIN BINDING; PROTEIN CONFORMATION; RATS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SPODOPTERA; SURFACE PLASMON RESONANCE; TIME;

EID: 62949196901     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-008-0384-y     Document Type: Article
Times cited : (34)

References (36)
  • 1
    • 15844369794 scopus 로고    scopus 로고
    • Surface plasmon resonance for the analysis of β-amyloid interactions and fibril formation in Alzheimer's disease research
    • M-I Aguilar DH Small 2005 Surface plasmon resonance for the analysis of β-amyloid interactions and fibril formation in Alzheimer's disease research Neurotox Res 7 17 27
    • (2005) Neurotox Res , vol.7 , pp. 17-27
    • Aguilar, M.-I.1    Small, D.H.2
  • 2
    • 1342322692 scopus 로고    scopus 로고
    • Conformational changes of beta-lactoglobulin in sodium bis(2-ethylhexyl) sulfosuccinate reverse micelles. A fluorescence and CD study
    • 10.1111/j.1432-1033.2004.03977.x
    • SM Andrade TI Carvalho MI Viseu SM Costa 2004 Conformational changes of beta-lactoglobulin in sodium bis(2-ethylhexyl) sulfosuccinate reverse micelles. A fluorescence and CD study Eur J Biochem 271 734 744 10.1111/j.1432-1033.2004. 03977.x
    • (2004) Eur J Biochem , vol.271 , pp. 734-744
    • Andrade, S.M.1    Carvalho, T.I.2    Viseu, M.I.3    Costa, S.M.4
  • 4
    • 62949126672 scopus 로고    scopus 로고
    • Real-time binding kinetics monitored with surface plasmon resonance imaging in a diffusion-free environment
    • 10.2174/1874383800802010001
    • R D'Agata G Grasso G Spoto 2008 Real-time binding kinetics monitored with surface plasmon resonance imaging in a diffusion-free environment Open Spectrosc J 2 1 9 10.2174/1874383800802010001
    • (2008) Open Spectrosc J , vol.2 , pp. 1-9
    • D'Agata, R.1    Grasso, G.2    Spoto, G.3
  • 5
    • 62949232115 scopus 로고
    • Scientific American Books New York
    • Darnell JE, Lodish H, Baltimore D (1990) Molecular cell biology. Scientific American Books, New York
    • (1990)
    • Darnell, J.E.1    Lodish, H.2    Baltimore, D.3
  • 9
    • 8444241450 scopus 로고    scopus 로고
    • Studies of substrate-induced conformational changes in human cytomegalovirus protease using optical biosensor technology
    • 10.1016/j.ab.2004.06.008
    • M Geitmann UH Danielson 2004 Studies of substrate-induced conformational changes in human cytomegalovirus protease using optical biosensor technology Anal Biochem 332 203 214 10.1016/j.ab.2004.06.008
    • (2004) Anal Biochem , vol.332 , pp. 203-214
    • Geitmann, M.1    Danielson, U.H.2
  • 12
    • 34247259490 scopus 로고    scopus 로고
    • A new methodology for monitoring the activity of cdMMP-12 anchored and freeze-dried on Au (111)
    • 10.1016/j.jasms.2007.02.003
    • G Grasso M Fragai E Rizzarelli G Spoto KJ Yeo 2007 A new methodology for monitoring the activity of cdMMP-12 anchored and freeze-dried on Au (111) J Am Soc Mass Spectrom 18 961 969 10.1016/j.jasms.2007.02.003
    • (2007) J Am Soc Mass Spectrom , vol.18 , pp. 961-969
    • Grasso, G.1    Fragai, M.2    Rizzarelli, E.3    Spoto, G.4    Yeo, K.J.5
  • 13
    • 38149007269 scopus 로고    scopus 로고
    • AP/MALDI-MS complete characterization of the proteolytic fragments produced by the interaction of insulin degrading enzyme with bovine insulin
    • 10.1002/jms.1348
    • G Grasso E Rizzarelli G Spoto 2007 AP/MALDI-MS complete characterization of the proteolytic fragments produced by the interaction of insulin degrading enzyme with bovine insulin J Mass Spectrom 42 1590 1598 10.1002/jms.1348
    • (2007) J Mass Spectrom , vol.42 , pp. 1590-1598
    • Grasso, G.1    Rizzarelli, E.2    Spoto, G.3
  • 14
    • 52449135535 scopus 로고    scopus 로고
    • How the binding and degrading capabilities of insulin degrading enzyme are affected by ubiquitin
    • G Grasso E Rizzarelli G Spoto 2008 How the binding and degrading capabilities of insulin degrading enzyme are affected by ubiquitin Biochim Biophys Acta 1784 1122 1126
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1122-1126
    • Grasso, G.1    Rizzarelli, E.2    Spoto, G.3
  • 15
    • 62949234361 scopus 로고    scopus 로고
    • Springer Berlin
    • Homola J (ed) (2006) Surface plasmon resonance based sensors. Springer, Berlin
    • (2006)
    • Homola, J.1
  • 16
    • 0036185561 scopus 로고    scopus 로고
    • Real-time kinetic analyses of the interaction of ricin toxin A-chain with ribosomes prove a conformational change involved in complex formation
    • E Honjo K Watanabe T Tsukamoto 2002 Real-time kinetic analyses of the interaction of ricin toxin A-chain with ribosomes prove a conformational change involved in complex formation J Biochem 131 267 275
    • (2002) J Biochem , vol.131 , pp. 267-275
    • Honjo, E.1    Watanabe, K.2    Tsukamoto, T.3
  • 19
    • 0032162964 scopus 로고    scopus 로고
    • Quantitative interpretation of the response of surface plasmon resonance sensors to adsorbed films
    • 10.1021/la971228b
    • LS Jung CT Campbell TM Chinowsky MN Mar SS Yee 1998 Quantitative interpretation of the response of surface plasmon resonance sensors to adsorbed films Langmuir 14 5636 5648 10.1021/la971228b
    • (1998) Langmuir , vol.14 , pp. 5636-5648
    • Jung, L.S.1    Campbell, C.T.2    Chinowsky, T.M.3    Mar, M.N.4    Yee, S.S.5
  • 20
    • 33749516129 scopus 로고    scopus 로고
    • Reversible pH-driven conformational switching of tethered superoxide dismutase with gold nanoparticle enhanced surface plasmon resonance spectroscopy
    • 10.1021/ja0632198
    • T Kang S Hong I Choi JJ Sung Y Kim J-S Hahn J Yi 2006 Reversible pH-driven conformational switching of tethered superoxide dismutase with gold nanoparticle enhanced surface plasmon resonance spectroscopy J Am Chem Soc 128 12870 12878 10.1021/ja0632198
    • (2006) J Am Chem Soc , vol.128 , pp. 12870-12878
    • Kang, T.1    Hong, S.2    Choi, I.3    Sung, J.J.4    Kim, Y.5    Hahn, J.-S.6    Yi, J.7
  • 21
    • 27844436113 scopus 로고    scopus 로고
    • Detection of bax protein conformational change using a surface plasmon resonance imaging-based antibody chip
    • 10.1016/j.bbrc.2005.10.155
    • M Kim SO Jung K Park E-J Jeong H-A Joung T-H Kim D-W Seol BH Chung 2005 Detection of bax protein conformational change using a surface plasmon resonance imaging-based antibody chip Biochem Biophys Res Commun 338 1834 1838 10.1016/j.bbrc.2005.10.155
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 1834-1838
    • Kim, M.1    Jung, S.O.2    Park, K.3    Jeong, E.-J.4    Joung, H.-A.5    Kim, T.-H.6    Seol, D.-W.7    Chung, B.H.8
  • 22
    • 0028176821 scopus 로고
    • Alzheimer's β-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme
    • 10.1016/0014-5793(94)00387-4
    • IV Kurochkin S Goto 1994 Alzheimer's β-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme FEBS Lett 345 33 37 10.1016/0014-5793(94)00387-4
    • (1994) FEBS Lett , vol.345 , pp. 33-37
    • Kurochkin, I.V.1    Goto, S.2
  • 23
    • 0033557842 scopus 로고    scopus 로고
    • A strategy for the generation of surfaces presenting ligands for studies of binding based on an active ester as a common reactive intermediate: A surface plasmon resonance study
    • 10.1021/ac980959t
    • J Lahiri L Isaacs J Tien GM Whitesides 1999 A strategy for the generation of surfaces presenting ligands for studies of binding based on an active ester as a common reactive intermediate: a surface plasmon resonance study Anal Chem 71 777 790 10.1021/ac980959t
    • (1999) Anal Chem , vol.71 , pp. 777-790
    • Lahiri, J.1    Isaacs, L.2    Tien, J.3    Whitesides, G.M.4
  • 24
    • 33750299577 scopus 로고    scopus 로고
    • Structural biology: Enzyme target to latch on to
    • 10.1038/nature05210
    • MA Leissring DJ Selkoe 2006 Structural biology: enzyme target to latch on to Nature 443 761 762 10.1038/nature05210
    • (2006) Nature , vol.443 , pp. 761-762
    • Leissring, M.A.1    Selkoe, D.J.2
  • 25
    • 84990436498 scopus 로고
    • Aqueous solutions containing amino acids and peptides. Part 20. Volumetric behavior of some terminally substituted amino acids and peptides at 298.15 K
    • 10.1002/bip.360240409
    • TE Leslie TH Lilley 1985 Aqueous solutions containing amino acids and peptides. Part 20. Volumetric behavior of some terminally substituted amino acids and peptides at 298.15 K Biopolymers 24 695 710 10.1002/bip.360240409
    • (1985) Biopolymers , vol.24 , pp. 695-710
    • Leslie, T.E.1    Lilley, T.H.2
  • 27
    • 39749194421 scopus 로고    scopus 로고
    • Immunocapture-based fluorometric assay for the measurement of insulin-degrading enzyme activity in brain tissue homogenates
    • 10.1016/j.jneumeth.2007.12.003
    • JS Miners PG Kehoe S Love 2008 Immunocapture-based fluorometric assay for the measurement of insulin-degrading enzyme activity in brain tissue homogenates J Neurosci Methods 169 177 181 10.1016/j.jneumeth.2007.12.003
    • (2008) J Neurosci Methods , vol.169 , pp. 177-181
    • Miners, J.S.1    Kehoe, P.G.2    Love, S.3
  • 28
    • 0031958764 scopus 로고    scopus 로고
    • CLAMP: A biosensor kinetic data analysis program
    • 10.1016/S0968-0004(98)01183-9
    • DG Myszka TA Morton 1998 CLAMP: a biosensor kinetic data analysis program Trends Biochem Sci 23 149 150 10.1016/S0968-0004(98)01183-9
    • (1998) Trends Biochem Sci , vol.23 , pp. 149-150
    • Myszka, D.G.1    Morton, T.A.2
  • 29
    • 0032831758 scopus 로고    scopus 로고
    • Analysis of fibril elongation using surface plasmon resonance biosensors
    • 10.1016/S0076-6879(99)09027-8
    • DG Myszka SJ Wood AL Biere 1999 Analysis of fibril elongation using surface plasmon resonance biosensors Methods Enzymol 309 386 402 10.1016/S0076-6879(99)09027-8
    • (1999) Methods Enzymol , vol.309 , pp. 386-402
    • Myszka, D.G.1    Wood, S.J.2    Biere, A.L.3
  • 30
    • 0026493924 scopus 로고
    • Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis
    • 10.1021/bi00159a003
    • AJ Sharff LE Rodseth JC Spurlino FA Quiocho 1992 Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis Biochemistry 31 10657 10663 10.1021/bi00159a003
    • (1992) Biochemistry , vol.31 , pp. 10657-10663
    • Sharff, A.J.1    Rodseth, L.E.2    Spurlino, J.C.3    Quiocho, F.A.4
  • 31
    • 33750302461 scopus 로고    scopus 로고
    • Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism
    • 10.1038/nature05143
    • Y Shen A Joachimiak MR Rosner W-J Tang 2006 Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism Nature 443 870 874 10.1038/nature05143
    • (2006) Nature , vol.443 , pp. 870-874
    • Shen, Y.1    Joachimiak, A.2    Rosner, M.R.3    Tang, W.-J.4
  • 32
    • 0348010388 scopus 로고    scopus 로고
    • Substrate activation of insulin degrading enzyme (insulysin), a potential target for drug development
    • 10.1074/jbc.M308983200
    • ES Song MA Juliano L Juliano LB Hersh 2003 Substrate activation of insulin degrading enzyme (insulysin), a potential target for drug development J Biol Chem 278 49789 49794 10.1074/jbc.M308983200
    • (2003) J Biol Chem , vol.278 , pp. 49789-49794
    • Song, E.S.1    Juliano, M.A.2    Juliano, L.3    Hersh, L.B.4
  • 33
    • 0032523411 scopus 로고    scopus 로고
    • Detection of conformational changes in an immobilized protein using surface plasmon resonance
    • 10.1021/ac9713666
    • H Sota Y Hasegawa M Iwakura 1998 Detection of conformational changes in an immobilized protein using surface plasmon resonance Anal Chem 70 2019 2024 10.1021/ac9713666
    • (1998) Anal Chem , vol.70 , pp. 2019-2024
    • Sota, H.1    Hasegawa, Y.2    Iwakura, M.3
  • 35
    • 0042510389 scopus 로고    scopus 로고
    • Measuring adsorption of a hydrophobic probe with a surface plasmon resonance sensor to monitor conformational changes in immobilized proteins
    • 10.1021/bp034015n
    • S Yamaguchi T Mannen T Zako N Kamiya T Nagamune 2003 Measuring adsorption of a hydrophobic probe with a surface plasmon resonance sensor to monitor conformational changes in immobilized proteins Biotechnol Prog 19 1348 1354 10.1021/bp034015n
    • (2003) Biotechnol Prog , vol.19 , pp. 1348-1354
    • Yamaguchi, S.1    Mannen, T.2    Zako, T.3    Kamiya, N.4    Nagamune, T.5
  • 36
    • 3342901819 scopus 로고    scopus 로고
    • Botulinum neurotoxin A changes conformation upon binding to ganglioside GT1b
    • 10.1021/bi0494673
    • BC Yowler C-L Schengrund 2004 Botulinum neurotoxin A changes conformation upon binding to ganglioside GT1b Biochemistry 43 9725 9731 10.1021/bi0494673
    • (2004) Biochemistry , vol.43 , pp. 9725-9731
    • Yowler, B.C.1    Schengrund, C.-L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.