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

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, highe...

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Main Authors: P. Chavalitshewinkoon, S. Leelaphiwat, P. Wilairat
Other Authors: Mahidol University
Format: Article
Published: 2018
Subjects:
Medicine
Online Access:https://repository.li.mahidol.ac.th/handle/123456789/9705
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spelling th-mahidol.97052018-02-27T11:28:07Z Partial purification and characterization of DNA topoisomerase II from Plasmodium falciparum. P. Chavalitshewinkoon S. Leelaphiwat P. Wilairat Mahidol University Medicine 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. 2018-02-27T04:28:07Z 2018-02-27T04:28:07Z 1994-03-01 Article The Southeast Asian journal of tropical medicine and public health. Vol.25, No.1 (1994), 32-36 01251562 2-s2.0-0028402745 https://repository.li.mahidol.ac.th/handle/123456789/9705 Mahidol University SCOPUS https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0028402745&origin=inward
institution Mahidol University
building Mahidol University Library
continent Asia
country Thailand
Thailand
content_provider Mahidol University Library
collection Mahidol University Institutional Repository
topic Medicine
spellingShingle Medicine
P. Chavalitshewinkoon
S. Leelaphiwat
P. Wilairat
Partial purification and characterization of DNA topoisomerase II from Plasmodium falciparum.
description 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.
author2 Mahidol University
author_facet Mahidol University
P. Chavalitshewinkoon
S. Leelaphiwat
P. Wilairat
format Article
author P. Chavalitshewinkoon
S. Leelaphiwat
P. Wilairat
author_sort P. Chavalitshewinkoon
title Partial purification and characterization of DNA topoisomerase II from Plasmodium falciparum.
title_short Partial purification and characterization of DNA topoisomerase II from Plasmodium falciparum.
title_full Partial purification and characterization of DNA topoisomerase II from Plasmodium falciparum.
title_fullStr Partial purification and characterization of DNA topoisomerase II from Plasmodium falciparum.
title_full_unstemmed Partial purification and characterization of DNA topoisomerase II from Plasmodium falciparum.
title_sort partial purification and characterization of dna topoisomerase ii from plasmodium falciparum.
publishDate 2018
url https://repository.li.mahidol.ac.th/handle/123456789/9705
_version_ 1763491178782654464

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