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

P. Chavalitshewinkoon; S. Leelaphiwat; P. Wilairat

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

P. Chavalitshewinkoon
, S. Leelaphiwat
, P. Wilairat

Mahidol University

Research output: Contribution to journal › Article › peer-review

9 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	32-36
Number of pages	5
Journal	Southeast Asian Journal of Tropical Medicine and Public Health
Volume	25
Issue number	1
Publication status	Published - Mar 1994
Externally published	Yes

Cite this

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abstract = "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.",

author = "P. Chavalitshewinkoon and S. Leelaphiwat and P. Wilairat",

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AU - Chavalitshewinkoon, P.

AU - Leelaphiwat, S.

AU - Wilairat, P.

PY - 1994/3

Y1 - 1994/3

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0028402745

M3 - Article

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AN - SCOPUS:0028402745

SN - 0125-1562

VL - 25

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EP - 36

JO - Southeast Asian Journal of Tropical Medicine and Public Health

JF - Southeast Asian Journal of Tropical Medicine and Public Health

IS - 1

ER -

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

Abstract

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