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Physical-Chemical Antibody Properties Determine Optimal Separation Modes for Protein A Removal

by Jie Chen, Elliot Haimes, Jenifer Tetrault, Yanyu Zhang, and Arthur Ley, PhD
Volume 5, Issue 3 (Fall 2006)

The diversity of the antibody-antigen interaction and our ability to manipulate this interaction has created an enormous potential for the discovery and development of IgG therapeutics and diagnostics. Along with the expanding clinical pipeline of antibody products, increasing efforts have been devoted to improving antibody production and purification procedures. In order to meet drug discovery needs with limited resources, the so called “flexible generic purification scheme” approach has been adopted to develop a robust manufacturing process that allows the application of similar operational conditions to different monoclonal antibody molecules…

Citation:
Chen J, Haimes E, Tetrault J, Zhang Y, Ley A. Physical-Chemical Antibody Properties Determine Optimal Separation Modes for Protein A Removal.
BioProcess J, 2006; 5(3): 47-53. https://doi.org/10.12665/J53.Chen.

 
The Use of Disposable Systems in the Manufacture of Biopharmaceuticals

by Derek Pendlebury, PhD
Volume 5, Issue 3 (Fall 2006)

Biopharmaceutical manufacturers are constantly seeking new ways to lower production costs, while simultaneously increasing cost effectiveness without sacrificing quality. The U.S. biotech industry has grown from $8 billion in 1992 to $30 billion in 2002. As productivity in biopharmaceutical manufacturing has increased, pressures to contain costs have mounted in the healthcare industry, coupled with increased demands by investors, which results in increased cost containment pressures on the industry as a whole. Some biotechnology products need to be produced in large quantities (hundreds of kilograms per year) to meet both current and expected demand. This requires significant manufacturing capacity, and makes the types of incremental process improvements commonly sought in chemical pharmaceutical processing an attractive proposition for biopharmaceutical manufacturing…

Citation:
Pendlebury D. The Use of Disposable Systems in the Manufacture of Biopharmaceuticals.
BioProcess J, 2006; 5(3): 54-58. https://doi.org/10.12665/J53.Pendlebury.

 
A Universal Platform for the Purification of Therapeutic Proteins Using Affinity Tags: The Use of Engineered Aminopeptidases for His-Tag Removal

by José Arnau, PhD and John Pedersen
Volume 5, Issue 3 (Fall 2006)

Current expression technologies have enabled the production of thousands of recombinant proteins in diverse production hosts. Therapeutic recombinant proteins have been engineered for a variety of purposes including reduced antigenicity, longer half-life, simplified process development, and increased affinity. Protein engineering has relied on various high throughput methods (e.g., directed evolution, phage display) to identify candidate proteins with the desired therapeutic properties. The physiological and biochemical diversity of native and engineered proteins reflects on the abundance of production hosts, expression tools, and different approaches for protein purification. Notably, a key step in high-throughput protein production is purification, which is a bottleneck where large numbers of samples are involved. Universal purification methods that can be applied to virtually any protein, and that are amenable to automation, can be used to address this problem…

Citation:
Arnau J, Pedersen J. A Universal Platform for the Purification of Therapeutic Proteins Using Affinity Tags: The Use of Engineered Aminopeptidases for His-Tag Removal.
BioProcess J, 2006; 5(3): 59-65. https://doi.org/10.12665/J53.Arnau.

 
Evaluation of Filtration Products in the Production of Adenovirus Candidates Used in Vaccine Production: Overview and Case Study

by Halima Namatovu, Wendy Hsu, Ruta Waghmare, Suneeta Wastler, Christi McDowell, and Bryan T. Butman
Volume 5, Issue 3 (Fall 2006)

Adenoviral vectors (AAV’s) offer a promising new approach to vaccine development. They have the ability to be rapidly manipulated for bearing transgenic coding for specific antigenic proteins, efficiently infect a variety of mammalian cell types (including antigen-presenting cells) and induce a broad immune response against the target antigen in vaccine recipients. Furthermore, AAV’s offer an excellent safety profile, in that they can be engineered to be non-replicating in the vaccine recipient and they lack the molecular mechanism for integration into the host genome. AAV’s are highly amenable to scalable manufacturing processes such as the use of stirred tank bioreactors, high capacity filtration methods, and chromatographic purification procedures…

Citation:
Namatovu H, Hsu W, Waghmare R, Wastler S, McDowell C, Butman BT. Evaluation of Filtration Products in the Production of Adenovirus Candidates Used in Vaccine Production: Overview and Case Study.
BioProcess J, 2006; 5(3): 67-74. https://doi.org/10.12665/J53.Namatovu.

 
Meeting the Challenges of IgG Expression: From Antibody Libraries to Clinical Supply

by Olalekan Daramola, Diane Hatton, and Ray Field
Volume 5, Issue 2 (Summer 2006)

A number of antibody drugs are currently in clinical development and 22 antibodies (including five diagnostic antibodies) have received FDA market approval in the last decade. A number of different technologies are now being used successfully to isolate potent therapeutic antibodies with minimal immunogenicity and improved safety. These include chimerisation (mouse/human antibodies), humanisation (complementarity-determining region [CDR] grafting), transgenic mice, phage display, ribosome display, and other emerging technologies. The phage and ribosome display technologies used at Cambridge Antibody Technology (CAT) are based on the physical linkage of gene to gene product which enables the recovery and enrichment of genetic material encoding the selected antibody...

Citation:
Daramola O, Hatton D, Field R. Meeting the Challenges of IgG Expression: From Antibody Libraries to Clinical Supply.
BioProcess J, 2006; 5(2): 21-25. https://doi.org/10.12665/J52.Daramola.

 
Characterization and Release of Raw Materials Used in Upstream Processes for Production of Monoclonal Antibodies by Mammalian Cell Culture

by Uma Balasubramanian, Peter Salmon, David Robinson, and Jinyou Zhang, PhD
Volume 5, Issue 2 (Summer 2006)

Since the mid-1970’s, when Kohler and Milstein first discovered the process by which myeloma cells and splenocytes could be fused to produce monoclonal antibodies (MAbs), a whole new world of important therapeutic, prophylactic and diagnostic products has opened up, bringing in huge benefits for patients and manufacturers. The total sales of therapeutic MAbs reached more than $13 billion in 2005. Sixteen of the 18 FDA-approved MAbs came to the market after 1997, and over 150 are currently in clinical development, suggesting their increasing medical importance and the remarkable, recent advancements in development technology...

Citation:
Balasubramanian U, Salmon P, Robinson D, Zhang J. Characterization and Release of Raw Materials Used in Upstream Processes for Production of Monoclonal Antibodies by Mammalian Cell Culture.
BioProcess J, 2006; 5(2): 7-13. https://doi.org/10.12665/J52.Balasubramanian.

 
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