Heat stability of lyophilized Cl inactivator (Cl-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 °C and for 10 h at
80, 90 and 100°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