Drosophihlatopoisomerase I: isolation, purificatioann and characterization | Zendy

Kashayar Javaherian | Zendy; Yuk-Ching Tse | Zendy; José M. Vega | Zendy

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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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