Activation of latent RNAase by antibodies against rat liver RNAase inhibitor.

RNAase inhibitor was purified to homogeneity from rat liver. The purified inhibitor was identified by measuring the activity in gel slices after polyacrylamide gel electrophoresis under non-denaturing conditions. Antibodies were prepared by immunization of guinea pigs with the inhibitor. The antibodies formed single precipitin lines with free RNAase inhibitor and RNAase A-inhibitor complex that fused in a micro-Ouchterlony test. Partially purified IgG from immunized animals, but not control animals, inhibited the activities of the free inhibitor and the inhibitor in the complex. In the latter case, the RNAase-inhibitor complex was dissociated and active RNAase was liberated.