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Characterization of the ATPase activity of topoisomerase II from Leishmania donovani and identification of residues conferring resistance to etoposide

We have cloned and expressed the 43 kDa N-terminal domain of Leishmania donovani topoisomerase II. This protein has an intrinsic ATPase activity and obeys Michaelis–Menten kinetics. Cross-linking studies indicate that the N-terminal domain exists as a dimer both in the presence and absence of nucleo...

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Библиографические подробности
Главные авторы: Sengupta, Tanushri, Mukherjee, Mandira, Das, Aditi, Mandal, Chhabinath, Das, Rakhee, Mukherjee, Tanmoy, Majumder, Hemanta K.
Формат: Artigo
Язык:Inglês
Опубликовано: Portland Press Ltd. 2005
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Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC1198921/
https://ncbi.nlm.nih.gov/pubmed/15901238
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1042/BJ20042128
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