Derlacz R A, Kowalska-Loth B, Staroń K
Institute of Biochemistry, Warsaw University, Warszawa, Poland.
Acta Biochim Pol. 1998;45(3):769-73.
Relaxing activity of Physarum topoisomerase I was increased by calf thymus protein kinase ck2, similarly as was the activity of mammalian topoisomerase I, despite a pronounced difference between amino-acid sequences of non-conserved domains of Physarum and mammalian enzymes. This feature of Physarum topoisomerase I was cancelled in nuclear extracts isolated from dibutyryl-cAMP treated plasmodia in which the activity of protein kinase ck2 was elevated.
多头绒泡菌拓扑异构酶I的松弛活性被小牛胸腺蛋白激酶CK2增强，哺乳动物拓扑异构酶I的活性也是如此，尽管多头绒泡菌和哺乳动物酶的非保守结构域的氨基酸序列存在明显差异。在从经二丁酰环磷腺苷处理的原质团中分离出的核提取物中，多头绒泡菌拓扑异构酶I的这一特性消失了，在该提取物中蛋白激酶CK2的活性升高。
