Abstract
Heat stability of lyophilized C1 inactivator (C1-INA) concentrates of intermediate and high purity has been investigated under several heat treatment protocols that include heating for 96 and 192 h at 68 degrees C and for 10 h at 80, 90 and 100 degrees C. Both types of concentrate showed high stability in functional activity, with not more than 5% loss in any of the time-temperature combinations evaluated. However, the C1-INA antigen from both concentrates showed small but progressive changes in crossed immunoelectrophoretic pattern, in proportion to the intensity of heat treatment. High-pressure size-exclusion chromatography revealed only minimal signs of aggregation in the high-purity concentrate, but a significant and progressive aggregation of nonspecific protein contaminants present in the intermediate-purity concentrate, making the high-purity concentrate preferable for heat treatment.
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