Purification of Caenorhabditis elegans DNA topoisomerase I

Sang Mee Park; Hyeon Sook Koo

doi:10.1016/0167-4781(94)90245-3

Purification of Caenorhabditis elegans DNA topoisomerase I

Sang Mee Park, Hyeon Sook Koo

Department of Biochemistry

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

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 language	English
Pages (from-to)	47-54
Number of pages	8
Journal	BBA - Gene Structure and Expression
Volume	1219
Issue number	1
DOIs	https://doi.org/10.1016/0167-4781(94)90245-3
Publication status	Published - 1994 Sept 13

Bibliographical note

Funding Information:
We thank Dr. Nam Jeong Cho (Chungbuk National University, Republic of Korea) for giving us C. elegans N2 and E. coli OP50. We are grateful to Drs. Leroy F. Liu and Peter D'Arpa (University of Medicine and Dentistry at New Jersey) for sending us rabbit antiserum against calf thymus DNA topoisomerase I. This work was supported by a Genetic Engineering Research Grant from the Ministry of Education, Korea.

All Science Journal Classification (ASJC) codes

Structural Biology
Biophysics
Biochemistry
Genetics

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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.",

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AB - 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.

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Purification of Caenorhabditis elegans DNA topoisomerase I

Abstract

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