Purification of Caenorhabditis elegans DNA topoisomerase I

Sang Mee Park, Hyeon Sook Koo

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

DNA topoisomerase I was partially purified from Caenorhabditis elegans worms. The enzyme is a 95 kDa polypeptide and its proteolytically degraded form of 70 kDa was also observed. The enzyme removed not only negative but also positive DNA supercoils. The optimum salt concentration for the DNA relaxation activity was 100 mM KCl, and divalent cations were not required but stimulated the activity. The DNA relaxation activity was weakly sensitive to 125 μM camptothecin but was completely inhibited by 125 μM berenil.

Original languageEnglish
Pages (from-to)47-54
Number of pages8
JournalBBA - Gene Structure and Expression
Volume1219
Issue number1
DOIs
Publication statusPublished - 1994 Sep 13

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Type I DNA Topoisomerase
Caenorhabditis elegans
Purification
DNA
Camptothecin
Divalent Cations
Enzymes
Salts
Peptides

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Genetics

Cite this

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Purification of Caenorhabditis elegans DNA topoisomerase I. / Park, Sang Mee; Koo, Hyeon Sook.

In: BBA - Gene Structure and Expression, Vol. 1219, No. 1, 13.09.1994, p. 47-54.

Research output: Contribution to journalArticle

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