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Drosophihlatopoisomerase I: isolation, purificatioann and characterization
Author(s) -
Kashayar Javaherian,
Yuk-Ching Tse,
José M. Vega
Publication year - 1982
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/10.21.6945
Subject(s) - biology , topoisomerase , enzyme , biochemistry , dna , dna supercoil , isolation (microbiology) , drosophila melanogaster , microbiology and biotechnology , gene , dna replication
We have purified and characterized topoisomerase I from Drosophila melanogaster. The molecular weight of the enzyme is 135,000; 100,000, 90,000, and 65,000 molecular weight products result from degradation of the enzyme. The enzyme relaxes both positive and negative supercoiled DNA. Mg++ is not absolutely required, but stimulates the enzymatic activity considerably.

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