Detection of RNAase inhibitor from different species and organs.

Human placental alkaline RNAase inhibitor was purified to homogeneity. Activity was measured after each purification step. The final identification of the purified protein was done by two-dimensional polyacrylamide gel electrophoresis and by immunoblotting. Antibodies were prepared by immunization of rabbits with the highly purified inhibitor. The availability of the antiserum directed against the human inhibitor enabled the detection of RNAase inhibitor from various other organs and species. This procedure has the advantage over the usual activity test in that the inhibitor can be found even if its activity has been lost.