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Volumn 406, Issue 28, 2014, Pages 7243-7251

Structural changes of ultrasonicated bovine serum albumin revealed by hydrogen-deuterium exchange and mass spectrometry

Author keywords

BSA structure; H D exchange; Mass spectrometry; Ultrasound

Indexed keywords

DEUTERIUM; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; HYDROGEN; MAMMALS; MASS SPECTROMETRY; PROTEINS; TUNNEL JUNCTIONS; ULTRASONICS;

EID: 84919754106     PISSN: 16182642     EISSN: 16182650     Source Type: Journal    
DOI: 10.1007/s00216-014-8136-6     Document Type: Article
Times cited : (18)

References (33)
  • 1
    • 0008121871 scopus 로고
    • Ultrasonic investigation of aqueous solutions of a globular protein
    • 1:CAS:528:DyaK38Xls12ksLg%3D
    • Pavlovskaya G, McClements D, Povey M (1992) Ultrasonic investigation of aqueous solutions of a globular protein. Food Hydrocoll 6(3):253-262. doi: 10.1016/S0268-005X(09)80093-3
    • (1992) Food Hydrocoll , vol.6 , Issue.3 , pp. 253-262
    • Pavlovskaya, G.1    McClements, D.2    Povey, M.3
  • 3
    • 0043161935 scopus 로고    scopus 로고
    • Conformational changes involved in thermal aggregation processes of bovine serum albumin
    • 1:CAS:528:DC%2BD3sXmsVejsbY%3D
    • Militello V, Vetri V, Leone M (2003) Conformational changes involved in thermal aggregation processes of bovine serum albumin. Biophys Chem 105(1):133-141. doi: 10.1016/s0301-4622(03)00153-4
    • (2003) Biophys Chem , vol.105 , Issue.1 , pp. 133-141
    • Militello, V.1    Vetri, V.2    Leone, M.3
  • 4
    • 7244256224 scopus 로고    scopus 로고
    • Sonication of proteins causes formation of aggregates that resemble amyloid
    • 1:CAS:528:DC%2BD2cXpsVWhtL0%3D
    • Stathopulos PB, Scholz GA, Hwang YM, Rumfeldt JAO, Lepock JR, Meiering EM (2004) Sonication of proteins causes formation of aggregates that resemble amyloid. Protein Sci 13(11):3017-3027. doi: 10.1110/Ps.04831804
    • (2004) Protein Sci , vol.13 , Issue.11 , pp. 3017-3027
    • Stathopulos, P.B.1    Scholz, G.A.2    Hwang, Y.M.3    Rumfeldt, J.A.O.4    Lepock, J.R.5    Meiering, E.M.6
  • 5
    • 33749386447 scopus 로고    scopus 로고
    • Structural and functional changes in ultrasonicated bovine serum albumin solutions
    • Gulseren I, Guzey D, Bruce BD, Weiss J (2007) Structural and functional changes in ultrasonicated bovine serum albumin solutions. Ultrason Sonochem 14(2):173-183. doi: 10.1016/j.ultsonch.2005.07.006
    • (2007) Ultrason Sonochem , vol.14 , Issue.2 , pp. 173-183
    • Gulseren, I.1    Guzey, D.2    Bruce, B.D.3    Weiss, J.4
  • 6
    • 32944482033 scopus 로고    scopus 로고
    • Interfacial properties and structural conformation of thermosonicated bovine serum albumin
    • Guzey D, Gulseren I, Bruce B, Weiss J (2006) Interfacial properties and structural conformation of thermosonicated bovine serum albumin. Food Hydrocoll 20(5):669-677. doi: 10.1016/j.foodhyd.2005.06.008
    • (2006) Food Hydrocoll , vol.20 , Issue.5 , pp. 669-677
    • Guzey, D.1    Gulseren, I.2    Bruce, B.3    Weiss, J.4
  • 7
    • 0034042912 scopus 로고    scopus 로고
    • The stability of enzymes after sonication
    • Özbek B, Ülgen K Ö. (2000) The stability of enzymes after sonication. Process Biochem 35(9):1037-1043. doi: 10.1016/S0032-9592(00)00141-2
    • (2000) Process Biochem , vol.35 , Issue.9 , pp. 1037-1043
    • Özbek, B.1    Ülgen, K.O.2
  • 8
    • 84884417939 scopus 로고    scopus 로고
    • Conformational changes of globular proteins adsorbed at oil-in-water emulsion interfaces examined by Synchrotron Radiation Circular Dichroism
    • 1:CAS:528:DC%2BC3sXltVaitw%3D%3D
    • Day L, Zhai J, Xu M, Jones NC, Hoffmann SV, Wooster TJ (2014) Conformational changes of globular proteins adsorbed at oil-in-water emulsion interfaces examined by Synchrotron Radiation Circular Dichroism. Food Hydrocoll 34:78-87. doi: 10.1016/j.foodhyd.2012.12.015
    • (2014) Food Hydrocoll , vol.34 , pp. 78-87
    • Day, L.1    Zhai, J.2    Xu, M.3    Jones, N.C.4    Hoffmann, S.V.5    Wooster, T.J.6
  • 9
    • 33646698223 scopus 로고    scopus 로고
    • Time-resolved fluorescence studies on bovine serum albumin denaturation process
    • 1:CAS:528:DC%2BD28XkvVWmsr0%3D
    • Togashi DM, Ryder AG (2006) Time-resolved fluorescence studies on bovine serum albumin denaturation process. J Fluoresc 16(2):153-160. doi: 10.1007/s10895-005-0029-9
    • (2006) J Fluoresc , vol.16 , Issue.2 , pp. 153-160
    • Togashi, D.M.1    Ryder, A.G.2
  • 10
    • 4444344985 scopus 로고    scopus 로고
    • Heat-induced secondary structure and conformation change of bovine serum albumin investigated by Fourier transform infrared spectroscopy
    • 1:CAS:528:DC%2BD2cXmslaqtrs%3D
    • Murayama K, Tomida M (2004) Heat-induced secondary structure and conformation change of bovine serum albumin investigated by Fourier transform infrared spectroscopy. Biochemistry-Us 43(36):11526-11532. doi: 10.1021/Bi0489154
    • (2004) Biochemistry-Us , vol.43 , Issue.36 , pp. 11526-11532
    • Murayama, K.1    Tomida, M.2
  • 11
    • 80053595948 scopus 로고    scopus 로고
    • New developments in protein structure-function analysis by MS and use of hydrogen-deuterium exchange microfluidics
    • 1:CAS:528:DC%2BC3MXhtlGksrfK
    • Landreh M, Astorga-Wells J, Johansson J, Bergman T, Jornvall H (2011) New developments in protein structure-function analysis by MS and use of hydrogen-deuterium exchange microfluidics. FEBS J 278(20):3815-3821. doi: 10.1111/j.1742-4658.2011.08215.x
    • (2011) FEBS J , vol.278 , Issue.20 , pp. 3815-3821
    • Landreh, M.1    Astorga-Wells, J.2    Johansson, J.3    Bergman, T.4    Jornvall, H.5
  • 13
    • 77953480345 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry: What is it and what can it tell us?
    • 1:CAS:528:DC%2BC3cXisFOks70%3D
    • Marcsisin SR, Engen JR (2010) Hydrogen exchange mass spectrometry: what is it and what can it tell us? Anal Biol Chem 397(3):967-972. doi: 10.1007/s00216-010-3556-4
    • (2010) Anal Biol Chem , vol.397 , Issue.3 , pp. 967-972
    • Marcsisin, S.R.1    Engen, J.R.2
  • 14
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • 1:CAS:528:DC%2BD28Xht12gs7k%3D
    • Wales TE, Engen JR (2006) Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrom Rev 25(1):158-170. doi: 10.1002/mas.20064
    • (2006) Mass Spectrom Rev , vol.25 , Issue.1 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 15
    • 80755144074 scopus 로고    scopus 로고
    • ExMS: Data analysis for HX-MS experiments
    • 1:CAS:528:DC%2BC3MXhtl2ns7nO
    • Kan ZY, Mayne L, Chetty PS, Englander SW (2011) ExMS: data analysis for HX-MS experiments. J Am Soc Mass Spectrom 22(11):1906-1915. doi: 10.1007/s13361-011-0236-3
    • (2011) J Am Soc Mass Spectrom , vol.22 , Issue.11 , pp. 1906-1915
    • Kan, Z.Y.1    Mayne, L.2    Chetty, P.S.3    Englander, S.W.4
  • 16
    • 0026096545 scopus 로고
    • Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe
    • 1:CAS:528:DyaK3MXhvVWmurY%3D
    • Semisotnov GV, Rodionova NA, Razgulyaev OI, Uversky VN, Gripas AF, Gilmanshin RI (1991) Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers 31(1):119-128. doi: 10.1002/bip.360310111
    • (1991) Biopolymers , vol.31 , Issue.1 , pp. 119-128
    • Semisotnov, G.V.1    Rodionova, N.A.2    Razgulyaev, O.I.3    Uversky, V.N.4    Gripas, A.F.5    Gilmanshin, R.I.6
  • 17
    • 0037009311 scopus 로고    scopus 로고
    • Interaction of drugs with bovine and human serum albumin
    • Sułkowska A (2002) Interaction of drugs with bovine and human serum albumin. J Mol Struct 614(1):227-232. doi: 10.1016/S0022-2860(02)00256-9
    • (2002) J Mol Struct , vol.614 , Issue.1 , pp. 227-232
    • Sułkowska, A.1
  • 18
    • 0021782306 scopus 로고
    • Serum albumin
    • 1:CAS:528:DyaL2MXmtV2js70%3D
    • Peters T Jr (1985) Serum albumin. Adv Protein Chem 37:161-245. doi: 10.1016/S0065-3233(08)60065-0
    • (1985) Adv Protein Chem , vol.37 , pp. 161-245
    • Peters, T.1
  • 19
    • 11244303574 scopus 로고    scopus 로고
    • Interaction of flavonoids with bovine serum albumin: A fluorescence quenching study
    • 1:CAS:528:DC%2BD2cXhtVOhsb%2FM
    • Papadopoulou A, Green RJ, Frazier RA (2005) Interaction of flavonoids with bovine serum albumin: a fluorescence quenching study. J Agric Food Chem 53(1):158-163. doi: 10.1021/jf048693g
    • (2005) J Agric Food Chem , vol.53 , Issue.1 , pp. 158-163
    • Papadopoulou, A.1    Green, R.J.2    Frazier, R.A.3
  • 20
    • 4143130272 scopus 로고    scopus 로고
    • Effect of guanidine hydrochloride on bovine serum albumin complex with antithyroid drugs: Fluorescence study
    • Sułkowska A, Rownicka J, Bojko B, Poźycka J, Zubik-Skupień I, Sułkowski W (2004) Effect of guanidine hydrochloride on bovine serum albumin complex with antithyroid drugs: fluorescence study. J Mol Struct 704(1):291-295. doi: 10.1016/j.molstruc.2003.12.065
    • (2004) J Mol Struct , vol.704 , Issue.1 , pp. 291-295
    • Sułkowska, A.1    Rownicka, J.2    Bojko, B.3    Poźycka, J.4    Zubik-Skupień, I.5    Sułkowski, W.6
  • 21
    • 0031852954 scopus 로고    scopus 로고
    • Unfolding of acrylodan-labeled human serum albumin probed by steady-state and time-resolved fluorescence methods
    • 1:CAS:528:DyaK1cXltFyiurg%3D
    • Flora K, Brennan JD, Baker GA, Doody MA, Bright FV (1998) Unfolding of acrylodan-labeled human serum albumin probed by steady-state and time-resolved fluorescence methods. Biophys J 75(2):1084-1096. doi: 10.1016/S0006-3495(98)77598-8
    • (1998) Biophys J , vol.75 , Issue.2 , pp. 1084-1096
    • Flora, K.1    Brennan, J.D.2    Baker, G.A.3    Doody, M.A.4    Bright, F.V.5
  • 22
    • 77950867479 scopus 로고    scopus 로고
    • Monitoring local unfolding of bovine serum albumin during denaturation using steady-state and time-resolved fluorescence spectroscopy
    • 1:CAS:528:DC%2BC3cXivFGnt7o%3D
    • Togashi DM, Ryder AG, O'Shaughnessy D (2010) Monitoring local unfolding of bovine serum albumin during denaturation using steady-state and time-resolved fluorescence spectroscopy. J Fluoresc 20(2):441-452. doi: 10.1007/s10895-009-0566-8
    • (2010) J Fluoresc , vol.20 , Issue.2 , pp. 441-452
    • Togashi, D.M.1    Ryder, A.G.2    O'Shaughnessy, D.3
  • 23
    • 0026116076 scopus 로고
    • Solvent-induced conformational changes of polypeptides probed by electrospray-ionization mass spectrometry
    • 1:CAS:528:DyaK3MXhvVWmurs%3D
    • Loo JA, Loo RR, Udseth HR, Edmonds CG, Smith RD (1991) Solvent-induced conformational changes of polypeptides probed by electrospray-ionization mass spectrometry. Rapid Commun Mass Spectrom: RCM 5(3):101-105. doi: 10.1002/rcm.1290050303
    • (1991) Rapid Commun Mass Spectrom: RCM , vol.5 , Issue.3 , pp. 101-105
    • Loo, J.A.1    Loo, R.R.2    Udseth, H.R.3    Edmonds, C.G.4    Smith, R.D.5
  • 24
    • 0035886952 scopus 로고    scopus 로고
    • Detection of multiple protein conformational ensembles in solution via deconvolution of charge-state distributions in ESI MS
    • 1:CAS:528:DC%2BD3MXmslOhtbw%3D
    • Dobo A, Kaltashov IA (2001) Detection of multiple protein conformational ensembles in solution via deconvolution of charge-state distributions in ESI MS. Anal Chem 73(20):4763-4773. doi: 10.1021/ac010713f
    • (2001) Anal Chem , vol.73 , Issue.20 , pp. 4763-4773
    • Dobo, A.1    Kaltashov, I.A.2
  • 25
    • 0001754676 scopus 로고
    • Charge state distribution shifting of protein ions observed in matrix-assisted laser desorption ionization mass spectrometry
    • 1:CAS:528:DyaK28XhtVKltw%3D%3D
    • Zhou J, Lee TD (1995) Charge state distribution shifting of protein ions observed in matrix-assisted laser desorption ionization mass spectrometry. J Am Soc Mass Spectrom 6(12):1183-1189. doi: 10.1016/1044-0305(95)00578-1
    • (1995) J Am Soc Mass Spectrom , vol.6 , Issue.12 , pp. 1183-1189
    • Zhou, J.1    Lee, T.D.2
  • 26
    • 34548719814 scopus 로고    scopus 로고
    • Protein desolvation in UV matrix-assisted laser desorption/ionization (MALDI)
    • 1:CAS:528:DC%2BD2sXhtVOmu73P
    • Sachon E, Clodic G, Blasco T, Bolbach G (2007) Protein desolvation in UV matrix-assisted laser desorption/ionization (MALDI). J Am Soc Mass Spectrom 18(10):1880-1890. doi: 10.1016/j.jasms.2007.07.029
    • (2007) J Am Soc Mass Spectrom , vol.18 , Issue.10 , pp. 1880-1890
    • Sachon, E.1    Clodic, G.2    Blasco, T.3    Bolbach, G.4
  • 28
    • 84879825913 scopus 로고    scopus 로고
    • Glycation promoted by dynamic high pressure microfluidisation pretreatment revealed by high resolution mass spectrometry
    • 1:CAS:528:DC%2BC3sXhtFWrsL7E
    • Huang X, Tu Z, Wang H, Zhang Q, Hu Y, Zhang L, Niu P, Shi Y, Xiao H (2013) Glycation promoted by dynamic high pressure microfluidisation pretreatment revealed by high resolution mass spectrometry. Food Chem 141(3):3250-3259. doi: 10.1016/j.foodchem.2013.05.159
    • (2013) Food Chem , vol.141 , Issue.3 , pp. 3250-3259
    • Huang, X.1    Tu, Z.2    Wang, H.3    Zhang, Q.4    Hu, Y.5    Zhang, L.6    Niu, P.7    Shi, Y.8    Xiao, H.9
  • 29
    • 0031020684 scopus 로고    scopus 로고
    • Structure of pressure-induced denatured state of human serum albumin: A comparison with the intermediate in urea-induced denaturation
    • 1:CAS:528:DyaK2sXhsl2mtbo%3D
    • Tanaka N, Nishizawa H, Kunugi S (1997) Structure of pressure-induced denatured state of human serum albumin: a comparison with the intermediate in urea-induced denaturation. Biochim Biophys Acta 1338(1):13-20. doi: 10.1016/S0167-4838(96)00175-6
    • (1997) Biochim Biophys Acta , vol.1338 , Issue.1 , pp. 13-20
    • Tanaka, N.1    Nishizawa, H.2    Kunugi, S.3
  • 30
    • 20444424224 scopus 로고    scopus 로고
    • Guanidine hydrochloride denaturation of human serum albumin originates by local unfolding of some stable loops in domain III
    • 1:CAS:528:DC%2BD2MXltVOlsr0%3D
    • Ahmad B, Ahmed MZ, Haq SK, Khan RH (2005) Guanidine hydrochloride denaturation of human serum albumin originates by local unfolding of some stable loops in domain III. Biochim Biophys Acta 1750(1):93-102. doi: 10.1016/j.bbapap.2005.04.001
    • (2005) Biochim Biophys Acta , vol.1750 , Issue.1 , pp. 93-102
    • Ahmad, B.1    Ahmed, M.Z.2    Haq, S.K.3    Khan, R.H.4
  • 31
    • 37349070789 scopus 로고    scopus 로고
    • Effect of ultrasound treatment on solubility and foaming properties of whey protein suspensions
    • 1:CAS:528:DC%2BD1cXisFCltLs%3D
    • Jambrak AR, Mason TJ, Lelas V, Herceg Z, Herceg IL (2008) Effect of ultrasound treatment on solubility and foaming properties of whey protein suspensions. J Food Eng 86(2):281-287. doi: 10.1016/j.jfoodeng.2007.10.004
    • (2008) J Food Eng , vol.86 , Issue.2 , pp. 281-287
    • Jambrak, A.R.1    Mason, T.J.2    Lelas, V.3    Herceg, Z.4    Herceg, I.L.5
  • 32
    • 0032053268 scopus 로고    scopus 로고
    • Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey
    • 1:CAS:528:DyaK1cXltVOksrs%3D
    • Bryant CM, McClements DJ (1998) Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey. Trends Food Sci Technol 9(4):143-151. doi: 10.1016/S0924-2244(98)00031-4
    • (1998) Trends Food Sci Technol , vol.9 , Issue.4 , pp. 143-151
    • Bryant, C.M.1    McClements, D.J.2
  • 33
    • 84883480405 scopus 로고    scopus 로고
    • Effect of ultrasound treatment on particle size and molecular weight of whey proteins
    • 1:CAS:528:DC%2BC3sXhsVylsbrM
    • Jambrak AR, Mason TJ, Lelas V, Paniwnyk L, Herceg Z (2014) Effect of ultrasound treatment on particle size and molecular weight of whey proteins. J Food Eng 121:15-23. doi: 10.1016/j.jfoodeng.2013.08.012
    • (2014) J Food Eng , vol.121 , pp. 15-23
    • Jambrak, A.R.1    Mason, T.J.2    Lelas, V.3    Paniwnyk, L.4    Herceg, Z.5


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