메뉴 건너뛰기




Volumn 85, Issue 3, 2013, Pages 1591-1596

Studies of pH-dependent self-association of a recombinant form of arylsulfatase a with electrospray ionization mass spectrometry and size-exclusion chromatography

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC ENVIRONMENT; ALKALINE PH; ARYLSULFATASE; ASSEMBLY PROCESS; COOPERATIVE PROCESS; ELECTROSPRAY IONIZATION MASS SPECTROMETRY; ENDOGENOUS ENZYME; ENZYME REPLACEMENT THERAPY; HEXAMERS; HOMODIMERS; INTERCONVERSIONS; INTERMEDIATE SPECIE; INTERMEDIATE STATE; NEURODEGENERATIVE; NEUTRAL PH; OCTAMERS; PERIPHERAL NERVOUS SYSTEM; PH RANGE; PH-DEPENDENT; PROTEIN CONCENTRATIONS; RETENTION TIME; SELF-ASSOCIATIONS; SOLUTION PH; TETRAMERS; TIME-SCALES; TRANSITION STATE;

EID: 84873333987     PISSN: 00032700     EISSN: 15206882     Source Type: Journal    
DOI: 10.1021/ac302829k     Document Type: Article
Times cited : (23)

References (28)
  • 1
    • 7744245461 scopus 로고    scopus 로고
    • Accumulation of sulfatide in neuronal and glial cells of arylsulfatase A deficient mice
    • DOI 10.1023/B:NEUR.0000046572.53905.2c
    • Molander-Melin, M.; Pernber, Z.; Franken, S.; Gieselmann, V.; Mansson, J.-E.; Fredman, P. Accumulation of sulfatide in neuronal and glial cells of arylsulfatase A deficient mice J. Neurocytol. 2004, 33, 417-427 (Pubitemid 39463164)
    • (2004) Journal of Neurocytology , vol.33 , Issue.4 , pp. 417-427
    • Molander-Melin, M.1    Pernber, Z.2    Franken, S.3    Gieselmann, V.4    Mansson, J.-E.5    Fredman, P.6
  • 3
    • 84855354899 scopus 로고    scopus 로고
    • Developing treatment options for metachromatic leukodystrophy
    • Batzios, S. P.; Zafeiriou, D. I. Developing treatment options for metachromatic leukodystrophy Mol. Genet. Metab. 2012, 105, 56-63
    • (2012) Mol. Genet. Metab. , vol.105 , pp. 56-63
    • Batzios, S.P.1    Zafeiriou, D.I.2
  • 4
    • 33947640501 scopus 로고    scopus 로고
    • Enzyme, cell and gene-based therapies for metachromatic leukodystrophy
    • DOI 10.1007/s10545-007-0540-z
    • Sevin, C.; Aubourg, P.; Cartier, N. Enzyme, cell and gene-based therapies for metachromatic leukodystrophy J. Inherited Metab. Dis. 2007, 30, 175-183 (Pubitemid 46487998)
    • (2007) Journal of Inherited Metabolic Disease , vol.30 , Issue.2 , pp. 175-183
    • Sevin, C.1    Aubourg, P.2    Cartier, N.3
  • 5
    • 0036932518 scopus 로고    scopus 로고
    • Driving forces of protein association: The dimer-octamer equilibrium in arylsulfatase A
    • Vagedes, P.; Saenger, W.; Knapp, E.-W. Driving forces of protein association: The dimer-octamer equilibrium in arylsulfatase A Biophys. J. 2002, 83, 3066-3078 (Pubitemid 36041929)
    • (2002) Biophysical Journal , vol.83 , Issue.6 , pp. 3066-3078
    • Vagedes, P.1    Saenger, W.2    Knapp, E.-W.3
  • 6
    • 0037088685 scopus 로고    scopus 로고
    • Defective oligomerization of arylsulfatase A as a cause of its instability in lysosomes and metachromatic leukodystrophy
    • DOI 10.1074/jbc.M111993200
    • von Bülow, R.; Schmidt, B.; Dierks, T.; Schwabauer, N.; Schilling, K.; Weber, E.; Usón, I.; von Figura, K. Defective oligomerization of arylsulfatase A as a cause of its instability in lysosomes and metachromatic leukodystrophy J. Biol. Chem. 2002, 277, 9455-9461 (Pubitemid 34953032)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.11 , pp. 9455-9461
    • Von Low, R.B.1    Schmidt, B.2    Dierks, T.3    Schwabauer, N.4    Schilling, K.5    Weber, E.6    Uson, I.7    Von Figura, K.8
  • 7
    • 0032539976 scopus 로고    scopus 로고
    • Crystal structure of human arylsulfatase A: The aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis
    • DOI 10.1021/bi9714924
    • Lukatela, G.; Krauss, N.; Theis, K.; Selmer, T.; Gieselmann, V.; von Figura, K.; Saenger, W. Crystal structure of human arylsulfatase A: The aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis Biochemistry 1998, 37, 3654-3664 (Pubitemid 28162920)
    • (1998) Biochemistry , vol.37 , Issue.11 , pp. 3654-3664
    • Lukatela, G.1    Krauss, N.2    Theis, K.3    Selmer, T.4    Gieseimann, V.5    Von Figura, K.6    Saenger, W.7
  • 8
    • 0034030745 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analysis of a new crystal form of arylsulfatase A isolated from human placenta
    • DOI 10.1107/S0907444900003085
    • Lewinski, K.; Chruszcz, M.; Ksiazek, D.; Laidler, P. Crystallization and preliminary crystallographic analysis of a new crystal form of arylsulfatase A isolated from human placenta Acta Crystallogr., Sect. D: Biol. Crystallogr. 2000, 56, 650-652 (Pubitemid 30324833)
    • (2000) Acta Crystallographica Section D: Biological Crystallography , vol.56 , Issue.5 , pp. 650-652
    • Lewinski, K.1    Chruszcz, M.2    Ksiazek, D.3    Laidler, P.4
  • 9
    • 40749096882 scopus 로고    scopus 로고
    • Real-Time Monitoring of Protein Complexes Reveals their Quaternary Organization and Dynamics
    • DOI 10.1016/j.chembiol.2008.01.009, PII S1074552108000495
    • Painter, A. J.; Jaya, N.; Basha, E.; Vierling, E.; Robinson, C. V.; Benesch, J. L. P. Real-time monitoring of protein complexes reveals their quaternary organization and dynamics Chem. Biol. 2008, 15, 246-253 (Pubitemid 351381986)
    • (2008) Chemistry and Biology , vol.15 , Issue.3 , pp. 246-253
    • Painter, A.J.1    Jaya, N.2    Basha, E.3    Vierling, E.4    Robinson, C.V.5    Benesch, J.L.P.6
  • 10
    • 56149087277 scopus 로고    scopus 로고
    • Native mass spectrometry: A bridge between interactomics and structural biology
    • Heck, A. J. R. Native mass spectrometry: a bridge between interactomics and structural biology Nat. Meth. 2008, 5, 927-933
    • (2008) Nat. Meth. , vol.5 , pp. 927-933
    • Heck, A.J.R.1
  • 11
    • 76749099328 scopus 로고    scopus 로고
    • Conformation and dynamics of biopharmaceuticals: Transition of mass spectrometry-based tools from academe to industry
    • Kaltashov, I. A.; Bobst, C. E.; Abzalimov, R. R.; Berkowitz, S. A.; Houde, D. Conformation and dynamics of biopharmaceuticals: transition of mass spectrometry-based tools from academe to industry J. Am. Soc. Mass Spectrom. 2010, 21, 323-337
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 323-337
    • Kaltashov, I.A.1    Bobst, C.E.2    Abzalimov, R.R.3    Berkowitz, S.A.4    Houde, D.5
  • 12
    • 80052358612 scopus 로고    scopus 로고
    • Advanced Mass Spectrometry-Based Methods for the Analysis of Conformational Integrity of Biopharmaceutical Products
    • Bobst, C. E.; Kaltashov, I. A. Advanced Mass Spectrometry-Based Methods for the Analysis of Conformational Integrity of Biopharmaceutical Products Curr. Pharm. Biotechnol. 2011, 12, 1517-1529
    • (2011) Curr. Pharm. Biotechnol. , vol.12 , pp. 1517-1529
    • Bobst, C.E.1    Kaltashov, I.A.2
  • 13
    • 84855740330 scopus 로고    scopus 로고
    • Advances and challenges in analytical characterization of biotechnology products: Mass spectrometry-based approaches to study properties and behavior of protein therapeutics
    • Kaltashov, I. A.; Bobst, C. E.; Abzalimov, R. R.; Wang, G.; Baykal, B.; Wang, S. Advances and challenges in analytical characterization of biotechnology products: Mass spectrometry-based approaches to study properties and behavior of protein therapeutics Biotechnol. Adv. 2012, 30, 210-222
    • (2012) Biotechnol. Adv. , vol.30 , pp. 210-222
    • Kaltashov, I.A.1    Bobst, C.E.2    Abzalimov, R.R.3    Wang, G.4    Baykal, B.5    Wang, S.6
  • 14
    • 77957333488 scopus 로고    scopus 로고
    • Mass spectrometric analysis of intact human monoclonal antibody aggregates fractionated by size-exclusion chromatography
    • Kükrer, B.; Filipe, V.; van Duijn, E.; Kasper, P.; Vreeken, R.; Heck, A.; Jiskoot, W. Mass spectrometric analysis of intact human monoclonal antibody aggregates fractionated by size-exclusion chromatography Pharm. Res. 2010, 27, 2197-2204
    • (2010) Pharm. Res. , vol.27 , pp. 2197-2204
    • Kükrer, B.1    Filipe, V.2    Van Duijn, E.3    Kasper, P.4    Vreeken, R.5    Heck, A.6    Jiskoot, W.7
  • 15
    • 79954556420 scopus 로고    scopus 로고
    • Direct monitoring of heat-stressed biopolymers with temperature- controlled electrospray ionization mass spectrometry
    • Wang, G.; Abzalimov, R. R.; Kaltashov, I. A. Direct monitoring of heat-stressed biopolymers with temperature-controlled electrospray ionization mass spectrometry Anal. Chem. 2011, 83, 2870-2876
    • (2011) Anal. Chem. , vol.83 , pp. 2870-2876
    • Wang, G.1    Abzalimov, R.R.2    Kaltashov, I.A.3
  • 16
    • 84863044985 scopus 로고    scopus 로고
    • Evaluation of electrospray ionization mass spectrometry as a tool for characterization of small soluble protein aggregates
    • Wang, G.; Johnson, A. J.; Kaltashov, I. A. Evaluation of electrospray ionization mass spectrometry as a tool for characterization of small soluble protein aggregates Anal. Chem. 2012, 84, 1718-1724
    • (2012) Anal. Chem. , vol.84 , pp. 1718-1724
    • Wang, G.1    Johnson, A.J.2    Kaltashov, I.A.3
  • 17
    • 77956601839 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry of highly heterogeneous protein systems: Protein ion charge state assignment via incomplete charge reduction
    • Abzalimov, R. R.; Kaltashov, I. A. Electrospray ionization mass spectrometry of highly heterogeneous protein systems: Protein ion charge state assignment via incomplete charge reduction Anal. Chem. 2010, 82, 7523-7526
    • (2010) Anal. Chem. , vol.82 , pp. 7523-7526
    • Abzalimov, R.R.1    Kaltashov, I.A.2
  • 18
    • 33748368713 scopus 로고    scopus 로고
    • Mass measurements of increased accuracy resolve heterogeneous populations of intact ribosomes
    • DOI 10.1021/ja061468q
    • McKay, A. R.; Ruotolo, B. T.; Ilag, L. L.; Robinson, C. V. Mass measurements of increased accuracy resolve heterogeneous populations of intact ribosomes J. Am. Chem. Soc. 2006, 128, 11433-11442 (Pubitemid 44338835)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.35 , pp. 11433-11442
    • McKay, A.R.1    Ruotolo, B.T.2    Ilag, L.L.3    Robinson, C.V.4
  • 19
    • 79954609270 scopus 로고    scopus 로고
    • Interpreting the charge state assignment in electrospray mass spectra of bioparticles
    • Tseng, Y.-H.; Uetrecht, C.; Heck, A. J. R.; Peng, W.-P. Interpreting the charge state assignment in electrospray mass spectra of bioparticles Anal. Chem. 2011, 83, 1960-1968
    • (2011) Anal. Chem. , vol.83 , pp. 1960-1968
    • Tseng, Y.-H.1    Uetrecht, C.2    Heck, A.J.R.3    Peng, W.-P.4
  • 20
    • 50849098485 scopus 로고    scopus 로고
    • Do ionic charges in ESI MS provide useful information on macromolecular structure?
    • Kaltashov, I. A.; Abzalimov, R. R. Do ionic charges in ESI MS provide useful information on macromolecular structure? J. Am. Soc. Mass Spectrom. 2008, 19, 1239-1246
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 1239-1246
    • Kaltashov, I.A.1    Abzalimov, R.R.2
  • 21
    • 84855856984 scopus 로고    scopus 로고
    • Modeling the Behavior of Coarse-Grained Polymer Chains in Charged Water Droplets: Implications for the Mechanism of Electrospray Ionization
    • Ahadi, E.; Konermann, L. Modeling the Behavior of Coarse-Grained Polymer Chains in Charged Water Droplets: Implications for the Mechanism of Electrospray Ionization J. Phys. Chem. B 2012, 116, 104-112
    • (2012) J. Phys. Chem. B , vol.116 , pp. 104-112
    • Ahadi, E.1    Konermann, L.2
  • 22
    • 0035886670 scopus 로고    scopus 로고
    • Electrochemically induced pH changes resulting in protein unfolding in the ion source of an electrospray mass spectrometer
    • DOI 10.1021/ac010545r
    • Konermann, L.; Silva, E. A.; Sogbein, O. F. Electrochemically induced pH changes resulting in protein unfolding in the ion source of an electrospray mass spectrometer Anal. Chem. 2001, 73, 4836-4844 (Pubitemid 32980105)
    • (2001) Analytical Chemistry , vol.73 , Issue.20 , pp. 4836-4844
    • Konermann, L.1    Silva, E.A.2    Sogbein, O.F.3
  • 23
    • 9144223196 scopus 로고    scopus 로고
    • On-line size-exclusion chromatography/mass spectrometry of low molecular mass heparin
    • DOI 10.1002/jms.723
    • Henriksen, J.; Ringborg, L. H.; Roepstorrf, P. On-line size-exclusion chromatography/mass spectrometry of low molecular mass heparin J. Mass Spectrom. 2004, 39, 1305-1312 (Pubitemid 39545980)
    • (2004) Journal of Mass Spectrometry , vol.39 , Issue.11 , pp. 1305-1312
    • Henriksen, J.1    Ringborg, L.H.2    Roepstorrf, P.3
  • 24
    • 67649232637 scopus 로고    scopus 로고
    • Size exclusion chromatography coupled to electrospray ionization mass spectrometry for analysis and quantitative characterization of arsenic interactions with peptides and proteins
    • Schmidt, A.-C.; Fahlbusch, B.; Otto, M. Size exclusion chromatography coupled to electrospray ionization mass spectrometry for analysis and quantitative characterization of arsenic interactions with peptides and proteins J. Mass Spectrom. 2009, 44, 898-910
    • (2009) J. Mass Spectrom. , vol.44 , pp. 898-910
    • Schmidt, A.-C.1    Fahlbusch, B.2    Otto, M.3
  • 25
    • 73649121674 scopus 로고    scopus 로고
    • A Perfect Couple: PLP/SEC/ESI-MS for the Accurate Determination of Propagation Rate Coefficients in Free Radical Polymerization
    • Gruendling, T.; Voll, D.; Guilhaus, M.; Barner-Kowollik, C. A Perfect Couple: PLP/SEC/ESI-MS for the Accurate Determination of Propagation Rate Coefficients in Free Radical Polymerization Macromol. Chem. Phys. 2010, 211, 80-90
    • (2010) Macromol. Chem. Phys. , vol.211 , pp. 80-90
    • Gruendling, T.1    Voll, D.2    Guilhaus, M.3    Barner-Kowollik, C.4
  • 27
    • 79957628617 scopus 로고    scopus 로고
    • Identification and characterization of pharmacological chaperones to correct enzyme deficiencies in lysosomal storage disorders
    • Valenzano, K. J.; Khanna, R.; Powe, A. C.; Boyd, R.; Lee, G.; Flanagan, J. J.; Benjamin, E. R. Identification and characterization of pharmacological chaperones to correct enzyme deficiencies in lysosomal storage disorders Assay Drug Dev. Technol. 2011, 9, 213-235
    • (2011) Assay Drug Dev. Technol. , vol.9 , pp. 213-235
    • Valenzano, K.J.1    Khanna, R.2    Powe, A.C.3    Boyd, R.4    Lee, G.5    Flanagan, J.J.6    Benjamin, E.R.7
  • 28
    • 84857065242 scopus 로고    scopus 로고
    • Complete sequence determination of hemoglobin from endangered feline species using a combined ESI-MS and X-ray crystallography approach
    • Guo, J.; Uppal, S.; Easthon, L. M.; Mueser, T. C.; Griffith, W. P. Complete sequence determination of hemoglobin from endangered feline species using a combined ESI-MS and X-ray crystallography approach Int. J. Mass Spectrom. 2012, 312, 70-77
    • (2012) Int. J. Mass Spectrom. , vol.312 , pp. 70-77
    • Guo, J.1    Uppal, S.2    Easthon, L.M.3    Mueser, T.C.4    Griffith, W.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.