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Download Analysis of Aggregates and Particles in Protein by Hanns-Christian Mahler, Wim Jiskoot PDF

By Hanns-Christian Mahler, Wim Jiskoot

Content material:
Chapter 1 The serious desire for strong Assays for Quantitation and Characterization of Aggregates of healing Proteins (pages 1–7): John F. wood worker, Barry Cherney and Amy S. Rosenberg
Chapter 2 Separation?Based Analytical tools for Measuring Protein Aggregation (pages 9–36): Jun Liu, Barthelemy Demeule and Steven J. Shire
Chapter three Laser mild Scattering?Based innovations Used for the Characterization of Protein Therapeutics (pages 37–60): John den Engelsman, Fabian Kebbel and Patrick Garidel
Chapter four on-line Detection equipment and rising concepts for Soluble Aggregates in Protein prescription drugs (pages 61–84): Tapan okay. Das
Chapter five Analytical easy methods to degree Subvisible Particulates (pages 85–115): Shawn Cao, Linda Narhi, Yijia Jiang and Rahul S. Rajan
Chapter 6 Detection of seen debris in Parenteral items (pages 117–132): Ronald Smulders, Hans Vos and Hanns?Christian Mahler
Chapter 7 Characterization of Aggregates and debris utilizing rising thoughts (pages 133–167): Hui Zhao, Manuel Diez, Atanas Koulov, Mariola Bozova, Markus Bluemel and Kurt Forrer
Chapter eight Ultraviolet Absorption Spectroscopy (pages 169–200): Reza Esfandiary and Charles Russell Middaugh
Chapter nine Fluorescence Spectroscopy to signify Protein Aggregates and debris (pages 201–226): Robert A. Poole, Andrea Hawe, Wim Jiskoot and Kevin Braeckmans
Chapter 10 Infrared Spectroscopy to represent Protein Aggregates (pages 227–248): Marco van de Weert and Lene Jorgensen
Chapter eleven Raman Microscopy for Characterization of debris (pages 249–267): Stefan Fischer, Oliver Valet and Markus Lankers
Chapter 12 Microscopic equipment for Particle Characterization in Protein prescription drugs (pages 269–302): Patrick Garidel, Andrea Herre and Werner Kliche
Chapter thirteen comparability of equipment for Soluble mixture Detection and dimension Characterization (pages 303–333): John S. Philo
Chapter 14 Protein Purification and its Relation to Protein Aggregation and debris (pages 335–367): Roberto Falkenstein, Stefan Hepbildikler, Wolfgang Kuhne, Thorsten Lemm, Hans Rogl, Eva Rosenberg, Gerhard iciness, Frank Zettl and Ralf Zippelius
Chapter 15 formula improvement and its Relation to Protein Aggregation and debris (pages 369–387): Miriam Printz and Wolfgang Friess

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9. Bee JS, Chiu D, Sawicki S, Stevenson JL, Chatterjee K, Freund E, Carpenter JF, Randolph TW. Monoclonal antibody interactions with micro- and nanoparticles: adsorption, aggregation, and accelerated stress studies. J Pharm Sci 2009;98:3218–3238. 10. Lu Y, Harding SE, Rowe AJ, Davis KG, Fish B, Varley P, Gee C, Mulot S. The effect of a point mutation on the stability of IgG4 as monitored by analytical ultracentrifugation. J Pharm Sci 2008;97:960–969. 11. Liu D, Ren D, Huang H, Dankberg J, Rosenfeld R, Cocco MJ, Li L, Brems DN, Remmele RL Jr.

Among all these techniques, the flow FFF technique that uses a cross flow to create a vertical field has been widely used and is most suitable for the separation of protein aggregates [37]. For most protein molecules, the size of aggregates is well below ∼ 1 μm, and therefore, the separation purely relies on the diffusion coefficient of the protein species. This is also known as normal mode FFF operation. In contrast, for protein particles that are larger than ∼ 1 μm in size, the diffusion effect is essentially negligible [36].

This method uses finite-element solutions of the Lamm equation by direct fitting of the velocity data [23]. The sedimentation coefficient distribution from this method has a much improved resolution and covers a broader size distribution, since it explicitly corrects for the broadening due to diffusion and all the scans can be used in the analysis. In addition, this method includes a sophisticated regularization routine to help in removing spurious peaks that are caused by the noise in the raw data.

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