By Terence Cartwright
This ebook covers all points of the recent applied sciences had to flip animal cells into an appropriate and reasonably-priced instrument for drug construction. This comprises editing them genetically in order that they produce the suitable product in excessive yield, getting them to develop reproducibly on an business scale, and extracting the mandatory product from them. It additionally covers organic questions of safety, and the verification of the chemical and organic nature of the protein drug produced. The paintings covers the newest advancements in all of those parts and the way all of them must be built-in for the layout of a good biotechnological construction method.
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The speed and efficiency with which different cell types are able to fold protein correctly is emerging as one of the determinants of protein secretion capacity. 8 The family of subtilisin-related proteases involved in the proteolytic processing of protein precursors in mammalian cells (reviewed by Smeekens, 1993) Protease Tissue Specificity Secretory Pathway Intracellular Localization pH Optimum PC2 Neuroendocrine tissue Regulated Secretory granules Acid PC3 (PCI) Neuroendocrine tissue Regulated Secretory granules Acid PACE (furin) Ubiquitous Constitutive Golgi apparatus Neutral PACE 4 Ubiquitous Constitutive Golgi apparatus Neutral PC4 Ubiquitous Constitutive Golgi apparatus Neutral engineer cells with the ideal chaperone molecule complement for maximizing expression of a given recombinant protein.
This 3'flankingcontrol sequence again drives high-level expression in a position-independent manner. Stimulation of expression by the use of vectors which incorporate dominant control regions clearly offers many advantages in terms of yield of protein, frequency of achieving productive clones and stability of production. It is very likely that other such regions associated with tissue-specific developmental expression of mammalian genes will be identified and that systems using these will become the method of choice for high-level expression of heterologous protein in animal cells.
Recently, Cossons et al (1991) reported progressive loss of gamma interferon production in amplified CHO cells maintained in the contin- 30 Yields of recombinant product uous presence of 100 nM methotrexate. Interferon titre fell by over 70% over 120 days in culture. During this time the level of DHFR DNA fell markedly, although the level of interferon DNA fell rather less. No major chromosomal changes were observed. In parallel with this loss of productivity, maximum cell density obtained increased and cell viability was maintained for longer periods, suggesting that a growth advantage was operating for cells which had partially lost the amplified sequences.