Publication:
Partial purification and characterization of DNA topoisomerase II from Plasmodium falciparum.

dc.contributor.authorP. Chavalitshewinkoonen_US
dc.contributor.authorS. Leelaphiwaten_US
dc.contributor.authorP. Wilairaten_US
dc.contributor.otherMahidol Universityen_US
dc.date.accessioned2018-02-27T04:28:07Z
dc.date.available2018-02-27T04:28:07Z
dc.date.issued1994-03-01en_US
dc.description.abstractDNA 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.en_US
dc.identifier.citationThe Southeast Asian journal of tropical medicine and public health. Vol.25, No.1 (1994), 32-36en_US
dc.identifier.issn01251562en_US
dc.identifier.other2-s2.0-0028402745en_US
dc.identifier.urihttps://repository.li.mahidol.ac.th/handle/123456789/9705
dc.rightsMahidol Universityen_US
dc.rights.holderSCOPUSen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0028402745&origin=inwarden_US
dc.subjectMedicineen_US
dc.titlePartial purification and characterization of DNA topoisomerase II from Plasmodium falciparum.en_US
dc.typeArticleen_US
dspace.entity.typePublication
mu.datasource.scopushttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0028402745&origin=inwarden_US

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