Coupling Multi Angle Light Scattering to Ion Exchange chromatography (IEX-MALS) for protein characterization.
作者： Hadar Amartely , Orly Avraham , Assaf Friedler , Oded Livnah , Mario Lebendiker
DOI: 10.1038/S41598-018-25246-6
关键词: Coupling 、 Characterization (materials science) 、 Light scattering 、 Multiangle light scattering 、 Ion exchange 、 Chemistry 、 Ion chromatography 、 Size-exclusion chromatography 、 Analytical chemistry 、 Resolution (mass spectrometry)
摘要: Multi-angle light scattering coupled with size exclusion chromatography (SEC-MALS) is a standard and common approach for characterizing protein mass, overall shape, aggregation, oligomerization, interactions purity. The limited resolution of analytical SEC restricts in some instances the accurate analysis that can be accomplished by MALS. These include mixtures populations identical or very similar molecular masses, oligomers poor separation short peptides. Here we show combining MALS higher technique ion exchange (IEX-MALS) allow precise analyses samples cannot resolved SEC-MALS. We conclude IEX-MALS valuable complementary method characterization, especially systems could not fully analyzed
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Erinc Sahin, Christopher J. Roberts, Size-Exclusion Chromatography with Multi-angle Light Scattering for Elucidating Protein Aggregation Mechanisms Methods of Molecular Biology. ,vol. 899, pp. 403- 423 ,(2012) , 10.1007/978-1-61779-921-1_25
Joanne E. Nettleship, James Brown, Matthew R. Groves, Arie Geerlof, Methods for Protein Characterization by Mass Spectrometry, Thermal Shift (ThermoFluor) Assay, and Multiangle or Static Light Scattering Methods in Molecular Biology. ,vol. 426, pp. 299- 318 ,(2008) , 10.1007/978-1-60327-058-8_19
Atsushi Hirano, Tsutomu Arakawa, Tomoshi Kameda, Effects of arginine on multimodal anion exchange chromatography. Protein Expression and Purification. ,vol. 116, pp. 105- 112 ,(2015) , 10.1016/J.PEP.2015.07.013
Orly Avraham, Amit Meir, Alexander Fish, Edward A. Bayer, Oded Livnah, Hoefavidin: A dimeric bacterial avidin with a C-terminal binding tail. Journal of Structural Biology. ,vol. 191, pp. 139- 148 ,(2015) , 10.1016/J.JSB.2015.06.020
Philip M. Cummins, Keith D. Rochfort, Brendan F. O’Connor, Ion-Exchange Chromatography: Basic Principles and Application Methods of Molecular Biology. ,vol. 1485, pp. 209- 223 ,(2017) , 10.1007/978-1-4939-6412-3_11
Sarah L. Dallas, Qian Chen, Pitchumani Sivakumar, Dynamics of Assembly and Reorganization of Extracellular Matrix Proteins Current Topics in Developmental Biology. ,vol. 75, pp. 1- 24 ,(2006) , 10.1016/S0070-2153(06)75001-3
Andrew D. NISBET, Richard H. SAUNDRY, Arthur J. G. MOIR, Linda A. FOTHERGILL, John E. FOTHERGILL, The Complete Amino-Acid Sequence of Hen Ovalbumin FEBS Journal. ,vol. 115, pp. 335- 345 ,(1981) , 10.1111/J.1432-1033.1981.TB05243.X
Timothy M. Pabst, Giorgio Carta, Natrajan Ramasubramanyan, Alan K. Hunter, Paul Mensah, Mark E. Gustafson, Separation of protein charge variants with induced pH gradients using anion exchange chromatographic columns. Biotechnology Progress. ,vol. 24, pp. 1096- 1106 ,(2008) , 10.1002/BTPR.53
Szabolcs Fekete, Alain Beck, Jean-Luc Veuthey, Davy Guillarme, Ion-exchange chromatography for the characterization of biopharmaceuticals Journal of Pharmaceutical and Biomedical Analysis. ,vol. 113, pp. 43- 55 ,(2015) , 10.1016/J.JPBA.2015.02.037
Lynne Reed Murphy, Nobuyuki Matubayasi, Vilia A Payne, Ronald M Levy, Protein hydration and unfolding--insights from experimental partial specific volumes and unfolded protein models. Folding and Design. ,vol. 3, pp. 105- 118 ,(1998) , 10.1016/S1359-0278(98)00016-9