Activation of topoisomerase II during partial purification by heparin-Sepharose chromatography

Fritz Boege*, Frank Gieseler, Michaela Müller, Harald Biersack, Peter Meyer

*Corresponding author for this work
5 Citations (Scopus)


Partial purification of topoisomerase II from small samples (107-108 cells) of human leukaemic cells was achieved by isolation of cell nuclei, hyper-osmotic extraction of nuclear proteins, sorption of nuclear proteins by heparin-Sepharose and elution with potassium phosphate. Similar results were obtained by gradient and batchwise elution. The catalytic activity of topoisomerase increased ca. eightfold after removal of ca. 95% of the contaminating nuclear proteins. The conserved enzymatic activity after partial purification indicates that the enzyme was not damaged. The half-life of enzymatic activity is increased by the chromatographic procedure. Owing to its high yield and technical simplicity, this could be a candidate procedure for the study of topoisomerase II in patient-derived blood samples.

Original languageEnglish
JournalJournal of Chromatography A
Issue number1
Pages (from-to)67-71
Number of pages5
Publication statusPublished - 13.11.1992


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