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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 severe desire for powerful 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 equipment for Measuring Protein Aggregation (pages 9–36): Jun Liu, Barthelemy Demeule and Steven J. Shire
Chapter three Laser mild Scattering?Based ideas 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 innovations for Soluble Aggregates in Protein prescription drugs (pages 61–84): Tapan okay. Das
Chapter five Analytical ways to 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 symbolize 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 prescribed 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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Additional info for Analysis of Aggregates and Particles in Protein Pharmaceuticals

Sample text

Importantly, characterization studies were conducted to ensure that the labeling process did not significantly alter the protein structure and function. 4 shows an example of omalizumab, a humanized anti-IgE mAb in human serum. 3 Sedimentation velocity analysis of an mAb in a liquid formulation after storage at −70 and 40◦ C for six months. The centrifuge experiments were conducted at 40,000 rpm and 10◦ C. The data were analyzed by SEDFIT using the continuous c(s) model. 4 Sedimentation velocity analysis of fluorescently labeled omalizumab in human serum.

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. This method has been widely used in the biopharmaceutical industry for monitoring the size distribution of aggregates.

The data were analyzed by SEDFIT using the continuous c(s) model. 4 Sedimentation velocity analysis of fluorescently labeled omalizumab in human serum. The experiments were conducted at 40,000 rpm and 25◦ C. The data were collected using a fluorescence detector, and the size distribution of the sedimentation coefficient was determined by SEDFIT using a continuous c(s) model. ANALYTICAL ULTRACENTRIFUGATION 23 was mixed with human serum, and sedimentation was monitored with a fluorescence detector. 2 s is the monomer peak of the mAb.

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