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  • aggregation  (3)
  • Springer  (3)
  • American Institute of Physics
  • American Institute of Physics (AIP)
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  • Springer  (3)
  • American Institute of Physics
  • American Institute of Physics (AIP)
  • Wiley-Blackwell  (2)
Years
  • 1
    Electronic Resource
    Electronic Resource
    Chaperone and foldase coexpression in the baculovirus-insect cell expression system (1996)
    Springer
    Cytotechnology 20 (1996), S. 149-159 
    Details
    ISSN: 1573-0778
    Keywords: aggregation ; BiP ; folding ; protein disulfide isomerase ; protein production ; secretion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Conclusions The BEVS has become widely utilized for production of recombinant proteins. However, protein aggregation and inefficient processing often limit yields, especially for secreted and membrane proteins. Since many proteins of pharmaceutical interest require similar posttranslational processing steps, engineering the folding, assembly, and secretion pathway may enhance the production of a wide variety of valuable complex proteins. Efforts should be undertaken to coexpress the relevant chaperones or foldases at low levels in concert with the final product to ensure the ideal folding and assembly environment. In the future, expression of oligosaccharide modifying enzymes and secretion factors may further improve secretion rates of assembled proteins and provide heterologous proteins with altered glycoforms. Also significant is the use of BEVS as an in vivo eucaryotic laboratory to study the fundamental roles of differnt chaperones, foldases, and secretion factors. The coexpression of chaperones and foldases will complement other approaches such as the development of alternative insect cell lines, promoters, and signal peptides to optimize the baculovirus-insect cell expression system for generating high yields of valuable proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00350396
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  • 2
    Electronic Resource
    Electronic Resource
    The Effect of Formulation Excipients on Protein Stability and Aerosol Performance of Spray-Dried Powders of a Recombinant Humanized Anti-IgE Monoclonal Antibody1 (1999)
    Springer
    Pharmaceutical research 16 (1999), S. 350-358 
    Details
    ISSN: 1573-904X
    Keywords: aggregation ; glycation ; fine particle fraction ; protein formulation ; protein stability ; spray drying
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Purpose. To study the effect of trehalose, lactose, and mannitol on the biochemical stability and aerosol performance of spray-dried powders of an anti-IgE humanized monoclonal antibody. Methods. Protein aggregation of spray-dried powders stored at various temperature and relative humidity conditions was assayed by size exclusion chromatography and sodium dodecyl sulfate polyacrylamide gel electrophoresis. Protein glycation was determined by isoelectric focusing and affinity chromatography. Crystallization was examined by X-ray powder diffraction. Aerosol performance was assessed as the fine particle fraction (FPF) of the powders blended with coarse carrier lactose, and was determined using a multiple stage liquid impinger. Results. Soluble protein aggregation consisting of non-covalent and disulfide-linked covalent dimers and trimers occurred during storage. Aggregate was minimized by formulation with trehalose at or above a molar ratio in the range of 300:1 to 500:1 (excipient:protein). However, the powders were excessively cohesive and unsuitable for aerosol administration. Lactose had a similar stabilizing effect, and the powders exhibited acceptable aerosol performance, but protein glycation was observed during storage. The addition of mannitol also reduced aggregation, while maintaining the FPF, but only up to a molar ratio of 200:1. Further increased mannitol resulted in crystallization, which had a detrimental effect on protein stability and aerosol performance. Conclusions. Protein stability was improved by formulation with carbohydrate. However, a balance must be achieved between the addition of enough stabilizer to improve protein biochemical stability without compromising blended powder aerosol performance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018805232453
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  • 3
    Electronic Resource
    Electronic Resource
    Stability of Interleukin 1β (IL-1β) in Aqueous Solution: Analytical Methods, Kinetics, Products, and Solution Formulation Implications (1991)
    Springer
    Pharmaceutical research 8 (1991), S. 485-490 
    Details
    ISSN: 1573-904X
    Keywords: interleukin 1β (IL-1β) ; protein stability ; analytical methodology ; aggregation ; denaturation ; autoxidation ; deamidation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The thermal stability of IL-1β in aqueous solution as a function of temperature (5–60°C), pH (2–9), buffer (acetate, citrate, tris, and phosphate), and cyroprotectants (sugars, HSA) was investigated in this study. The analytical methodologies included RP-HPLC, SEC, ELISA, IEF-PAGE, SDS-PAGE, and bioassay. The degradation and inactivation of IL-1β at or above 39°C were attributed to autoxidation of the two cysteine residues in the denatured protein, followed by hydrophobic/covalent aggregation and precipitation. At or below 30°C, IEF- and SDS-PAGE results suggest a possible deamidation reaction. The difference in mechanism of degradation precludes the prediction of formulation shelf life from accelerated temperature data. Nonetheless, the good stability observed at 5°C suggests that a solution formulation may be feasible for IL-1β.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1015851228163
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