Abstract
The loss of biological activity upon heating or agitation of human interferons is markedly altered by changing their aqueous environment. Low pH significantly stabilizes liquid fibroblast interferon at 68°C and 37°C whereas chaotropic salts stabilize at 68°C but not at 37°C; this anomalous result may be due to reactivation of biological activity at the higher temperature. The concentration of extraneous proteins influences the apparent thermal stability at any temperature and pH; thus, interferon was not stable even at low pH at protein concentrations less than 5 μg/ml. Solutions of partially purtially purified fibroblast interferon can be inactivated by mechanical stress; the addition of proteins or nonionic detergents prevents such inactivation. Freeze-dried preparations show the greatest thermal stability. The use of high-temperature, accelerated storage tests makes it possible to predict the shelf-life of freeze-dried interferon.
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References
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Sedmak, J.J., Jameson, P., Grossberg, S.E. (1978). Thermal and Vortical Stability of Purified Human Fibroblast Interferon. In: Stinebring, W.R., Chapple, P.J. (eds) Human Interferon. Advances in Experimental Medicine and Biology, vol 110. Springer, New York, NY. https://doi.org/10.1007/978-1-4615-9080-4_11
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DOI: https://doi.org/10.1007/978-1-4615-9080-4_11
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