Brown M, Dorson J W, Bollum F J
J Virol. 1973 Aug;12(2):203-8. doi: 10.1128/JVI.12.2.203-208.1973.
Purified vaccinia virus treated with Triton X-100 catalyzes the incorporation of ATP into an acid-insoluble product. The enzymatic activity responsible for the ATP polymerization is demonstrated to be different from vaccinia RNA polymerase in its preferential use of ATP as substrate and on the basis of heat stability, pH optima, and metal ion requirement. The ATP polymerization reaction is stimulated 10-fold by the addition of rA(pA)(5.) In accordance with our earlier terminology, we call this Mn(2+)-dependent enzyme terminal riboadenylate transferase to distinguish it from Mg(2+)-dependent poly A polymerase.
用曲拉通X-100处理的纯化痘苗病毒催化ATP掺入酸不溶性产物中。负责ATP聚合的酶活性在其对ATP作为底物的优先使用以及基于热稳定性、最适pH值和金属离子需求方面被证明与痘苗RNA聚合酶不同。通过添加rA(pA)(5.),ATP聚合反应被刺激了10倍。根据我们早期的术语,我们将这种依赖锰(2+)的酶称为末端核糖腺苷酸转移酶,以将其与依赖镁(2+)的多聚A聚合酶区分开来。