| Abstract: | An endoribonuclease has been purified about 320-fold from the microsomes of rat liver. The enzyme had an apparent molecular weight of 54 000-58 000 and produced oligonucleotides, each consisting of 3-7 nucleotides from poly(A) and poly(U). No mononucleotide was obtained by the enzymatic hydrolysis of poly(A) and poly(U) under standard coditions. The relative rates of breakdown of synthetic polynucleotides by the enzyme under standard conditions were in the order poly(U) = poly(A) > poly(C). Divalent cations (Mg2+ or Mn2+) was required for the enzymatic activity, but monovalent cations (Na+, K+ or NH4+) inhibited the enzyme. The breakdown of poly(C) and poly(U) by the enzyme was inhibited by spermine, but that of poly(A) was not influenced by spermine. The enzyme was inhibited by p-chloromercuribenzoate and poly(G), but not by rat-liver ribonuclease-inhibitor and anti-RNase A serum. |
