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Proteins, biopharmaceutical

APPLICATION OF SIZE EXCLUSION-HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY FOR BIOPHARMACEUTICAL PROTEIN AND PEPTIDE THERAPEUTICS... [Pg.531]

As well as overcoming many of the inherent problems associated with agriculture, plant tissue culture also offers a number of advantages over conventional animal cell culture methods currently being applied to produce biopharmaceutical proteins commercially [8], As plant culture media are relatively simple in composition and do not contain proteins, the cost of the process raw materials is reduced and protein recovery from the medium is easier and cheaper compared with animal cell culture. In addition, as most plant pathogens are unable to infect humans, the risk of pathogenic infections being transferred from the cell culture via the product is also substantially reduced. [Pg.16]

In this review, we focus on the use of plant tissue culture to produce foreign proteins that have direct commercial or medical applications. The development of large-scale plant tissue culture systems for the production of biopharmaceutical proteins requires efficient, high-level expression of stable, biologically active products. To minimize the cost of protein recovery and purification, it is preferable that the expression system releases the product in a form that can be harvested from the culture medium. In addition, the relevant bioprocessing issues associated with bioreactor culture of plant cells and tissues must be addressed. [Pg.16]

As indicated in Table 2.1, most of the promoters used in plant tissue culture have been based on the constitutive cauliflower mosaic virus (CaMV) 35S promoter. In contrast, inducible promoters have the advantage of allowing foreign proteins to be expressed at a time that is most conducive to protein accumulation and stability. Although a considerable number of inducible promoters has been developed and used in plant culture applications, e.g. [32-37], the only one to be applied thus far for the production of biopharmaceutical proteins is the rice a-amylase promoter. This promoter controls the production of an a-amylase isozyme that is one of the most abundant proteins secreted from cultured rice cells after sucrose starvation. The rice a-amylase promoter has been used for expression of hGM-CSF [10], aranti-trypsin [12, 29, 38, 39] and human lysozyme [30]. [Pg.25]

Biopharmaceutical proteins/Vaccines Gene Site erf Integration Promoter S /3 regulatory %tsp elements expression Laboratory... [Pg.117]

Proteins must be stable during processing, storage, and reconstitution (if lyo-philized). Although liquid formulation is preferred for protein biopharmaceuticals, it may not always be the most stable presentation. The biopharmaceutical protein may need to be lyophilized to maintain stability. Lyophilization involves the removal of water from a frozen substance by sublimation and water vaporization under vacuum.17 But in some cases, this process may itself cause protein instability. [Pg.292]

Another way to detect small molecules in the final formulated protein product without the interference from the protein signals is to remove the protein by ultrafiltration. Figure 12.4 compares a section of the proton NMR spectra of a biopharmaceutical protein product before (upper spectrum) and after (bottom spectrum) the protein was removed by ultrafiltering the sample with a Centricon-10 (Millipore Corp, Bedford, MA). Removing protein results in a flatter baseline (bottom spectrum). If small molecules are present in a protein sample, the removal of the protein may allow for unobstructed detection of the small molecules. In this case, a small amount of acetate ( 1 pg/rnl) is detected in the sample [bottom trace, Figure 12.4], Figure 12.5 shows that spikes of 10 p.g/ml of acetate and MES into the protein sample are fully recovered after the ultrafiltration to remove the protein. This example demonstrates that the interference of protein with the detection and quantitation of small-molecule impurities in a formulated protein product can be effectively eliminated by ultrafiltration. [Pg.315]

Figure 12.4 A section of the proton NMR spectra of a biopharmaceutical protein product before (upper spectrum) and after (bottom spectrum) the protein was removed by ultrafiltering the sample with Centricon-10. Figure 12.4 A section of the proton NMR spectra of a biopharmaceutical protein product before (upper spectrum) and after (bottom spectrum) the protein was removed by ultrafiltering the sample with Centricon-10.

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See also in sourсe #XX -- [ Pg.5 ]




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