Thermal and vortical stability of purified human fibroblast interferon.

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 degrees C and 37 degrees C whereas chaotropic salts stabilize at 68 degrees C but not at 37 degrees 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 microgram/ml. Solutions of partially 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.

journal_name

Adv Exp Med Biol

authors

Sedmak JJ,Jameson P,Grossberg SE

doi

10.1007/978-1-4615-9080-4_11

subject

Has Abstract

pub_date

1978-01-01 00:00:00

pages

133-52

eissn

0065-2598

issn

2214-8019

journal_volume

110

pub_type

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