The Southeast Asian journal of tropical medicine and public health. Vol.25, No.1 (1994), 32-36
Suggested Citation
P. Chavalitshewinkoon, S. Leelaphiwat, P. Wilairat Partial purification and characterization of DNA topoisomerase II from Plasmodium falciparum.. The Southeast Asian journal of tropical medicine and public health. Vol.25, No.1 (1994), 32-36. Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/9705
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Partial purification and characterization of DNA topoisomerase II from Plasmodium falciparum.
DNA topoisomerase II from Plasmodium falciparum was partially purified by FPLC using three columns: Econo-Pac Q, heparin-agarose and Mono Q. The enzyme showed ATP- and Mg2 +/- dependent activities in a decatenation assay, with optimum concentrations of 0.5 and 10 mM, respectively. Furthermore, highest activity was detected in the presence of 100 mM KCI. Enzyme decatenation activity was not inhibited by the DNA topoisomerase I inhibitor, camptothecin, but was sensitive to both prokaryotic and eukaryotic DNA topoisomerase II inhibitors.