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

By Hanns-Christian Mahler, Wim Jiskoot

ISBN-10: 0470497181

ISBN-13: 9780470497180

ISBN-10: 1118150570

ISBN-13: 9781118150573

Content material:
Chapter 1 The serious desire for powerful Assays for Quantitation and Characterization of Aggregates of healing Proteins (pages 1–7): John F. chippie, 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 gentle Scattering?Based recommendations 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 options for Soluble Aggregates in Protein prescribed drugs (pages 61–84): Tapan okay. Das
Chapter five Analytical how you can degree Subvisible Particulates (pages 85–115): Shawn Cao, Linda Narhi, Yijia Jiang and Rahul S. Rajan
Chapter 6 Detection of noticeable 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 tools for Soluble combination 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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Additional resources for Analysis of Aggregates and Particles in Protein Pharmaceuticals

Example text

The mobile phase should be filtered and degassed, since air bubbles or particles can damage the column and significantly increase the baseline noise and interfere with the UV, LS, and RI detection. To improve resolution, the protein sample should be relatively concentrated and the sample volume kept small (typically 1–5% of the column bed volume). The viscosity of the sample should not be significantly higher than the mobile phase buffer or peak broadening may occur. Higher flow rates will allow a faster separation; however, slower flow rates can result in better resolution of peaks.

The size of protein can be determined by directly comparing with MW standards. Native or nondenaturing gel electrophoresis has also been used to analyze proteins, particularly for those molecules where the native structure or biological activity needs to be maintained. The electrophoresis is conducted in the absence of denaturant, such as SDS. Therefore, it is possible to recover active proteins in their native state after the separation. The native gel electrophoresis separates proteins based on their sizes, conformation, and surface charges.

However, flow FFF also has several limitations. The separation of protein and aggregates is based on hydrodynamic properties, such as the diffusion coefficient, rather than the molecular mass. Therefore, an online LS detector is often connected to the flow FFF system to determine the molar mass of each species. The flow FFF system is also not suitable for the analysis of high-concentration protein solutions as the concentrated protein may form a viscous gel-like layer during the focusing and relaxation step and this would significantly compromise the resolution.

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