Sertic-Pritsos K, Vinocour M, Winicov I
Eur J Biochem. 1984 Oct 1;144(1):47-55. doi: 10.1111/j.1432-1033.1984.tb08429.x.
A 5'-hydroxyl RNA kinase from mouse L cells has been partially purified and characterized. The enzyme transfers the gamma-phosphorus from ATP to 5'-hydroxyl termini of RNA much more efficiently than DNA substrates, and is virtually inactive on 3'-CMP. The molecular mass of the predominant kinase activity is estimated to be 93-96 kDa from denaturing and non-denaturing polyacrylamide gel analyses. A minor band of lower molecular mass has been also observed. The enzyme activity requires Mg2+ and is inhibited by both Mn2+ and Zn2+. Antibodies to small nuclear ribonucleoproteins have no effect on this activity.
从小鼠L细胞中部分纯化并鉴定了一种5'-羟基RNA激酶。该酶将ATP的γ-磷酸基团转移到RNA的5'-羟基末端比转移到DNA底物上效率高得多，并且对3'-CMP几乎无活性。通过变性和非变性聚丙烯酰胺凝胶分析估计，主要激酶活性的分子量为93-96 kDa。还观察到一条低分子量的次要条带。该酶活性需要Mg2+，并受到Mn2+和Zn2+的抑制。针对小核核糖核蛋白的抗体对该活性没有影响。
