Observations on the kinetics of action of polyspermine-ribonuclease on poly(A).poly(U).

Starting from the observation that double-stranded ribonucleic acids are hydrolyzed more rapidly by bovine pancreatic ribonuclease that has been cross-linked to polyspermine, we have made an initial examination of the kinetics of the process. The addition of eight residues of the polyamine serves to strengthen the binding to poly(A).poly(U) 100-fold (Km changes from 2.7 . 10(-4) to 2.7 . 10(-6) M in total U) and to increase V for hydrolysis of the susceptible poly(U) strand from 2.5 to 16.2 delta A250 . min-1 per mg enzyme. There is evidence for inhibition by the RNAase-resistant poly(A) tracts in the substrate; free poly(A) shows a Ki of about 8 . 10(-6) M in total A.