Kumagai H, Igarashi K, Tanaka K, Nakao H, Hirose S
Biochim Biophys Acta. 1979 Jan 12;566(1):192-9. doi: 10.1016/0005-2744(79)90261-4.
A exoribonuclease has been purified from the microsomes of rat liver. The enzyme had an apparent molecular weight of 80 000-83 000 and produced, via a processive mechanism, 5'-AMP as the only product from poly(A). The degradation was found to proceed in the 3' to 5' direction. The relative rates of breakdown of synthetic polynucleotides by the enzyme under standard conditions were in the order poly(A) equal to poly(U) greater than poly(C). In addition to Mg2+, K+ was required for maximum activity. The enzymic activity was inhibited by p-chloromercuribenzoate and poly(G), but not by a rate liver RNAase inhibitor. The effect of spermine on the breakdown of synthetic polynucleotides by the enzyme has been studied. In the absence of K+, the breakdown of poly(C) was stimulated and that of poly(A) was stimulated slightly. However, the breakdown of poly(U) was inhibited slightly by spermine.
