By Hanns-Christian Mahler, Wim Jiskoot
Chapter 1 The severe 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 equipment for Measuring Protein Aggregation (pages 9–36): Jun Liu, Barthelemy Demeule and Steven J. Shire
Chapter three Laser gentle 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 tools and rising thoughts for Soluble Aggregates in Protein prescribed 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 innovations (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 signify 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 tools for Particle Characterization in Protein prescribed drugs (pages 269–302): Patrick Garidel, Andrea Herre and Werner Kliche
Chapter thirteen comparability of equipment 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 wintry weather, 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
This can have a signiﬁcant impact on the number of scans acquired during each experiment. The absorption optical system uses a Xenon ﬂash lamp, providing a usable wavelength range between 190 and 800 nm. The accuracy of the wavelength is calibrated with the spectrum of incident light or a wavelength reference cell that contains a holmium oxide ﬁlter. The typical accuracy of the wavelength is within ±3 nm. The interference optical system measures the protein concentration based on changes in RI.
The large protein aggregates beyond the upper size limit of the SEC column may be ﬁltered by the column matrix; therefore, it is important to assess sample recovery routinely. To avoid detector saturation and loss of resolution, high-concentration protein solutions are generally diluted even before injection onto the SEC column. This may interfere with the detection and characterization of concentration-dependent reversible aggregates. 14 SEPARATION-BASED ANALYTICAL METHODS The development of the SEC method usually includes selection of column matrix, elution buffers, injection volume/concentration, ﬂow rate, and column temperature.
Although there is no physical separation of protein species in centrifuge cells during sedimentation equilibrium experiments, sedimentation equilibrium and velocity methods are closely related. Thus, we include the discussion of both methods in this chapter. The sedimentation velocity experiment is usually conducted at relatively high rotor speeds and the centrifuge run only takes a few hours to complete. Each protein species can form a unique boundary and sediment at a characteristic speed under a speciﬁed centrifugal force on the basis of its molecular mass and shape.