Craine J E, Klee C B
Nucleic Acids Res. 1976 Nov;3(11):2923-8. doi: 10.1093/nar/3.11.2923.
We report here the presence of two enzymatic activities associated with highly purified preparations of polynucleotide phosphorylase from Micrococcus luteus. The first, a nuclease activity, which is not separated from the phosphorylase on hydroxylapatite, may be due to substitution of H2O for phosphate in the phosphorolysis reaction. The second activity, a deoxyadenylate kinase, the bulk of which is not resolved from the phosphorylase using gel filtration, sucrose density gradient centrifugation, DEAE-Sephadex, or hydroxylapatite chromatography, may represent a new activity of polynucleotide phosphorylase or be due to an enzyme which is tightly bound to the phosphorylase. Several properties of the kinase are described and its possible significance with respect to the overall enzyme mechanism is discussed.
我们在此报告,从藤黄微球菌中高度纯化得到的多核苷酸磷酸化酶制剂存在两种酶活性。第一种是核酸酶活性,在羟基磷灰石上它与磷酸化酶未分离,这可能是由于在磷酸解反应中水分子替代了磷酸基团所致。第二种活性是脱氧腺苷酸激酶,使用凝胶过滤、蔗糖密度梯度离心、DEAE - 葡聚糖凝胶或羟基磷灰石色谱法,其大部分与磷酸化酶无法分离,这可能代表多核苷酸磷酸化酶的一种新活性,或者是由于一种与磷酸化酶紧密结合的酶所致。文中描述了该激酶的几个特性,并讨论了其在整个酶作用机制方面可能具有的意义。