Separation of Topoisomerase I Activity from the Regulatory Subunit of Type II CyclicAdenosine Monophosphate-Dependent Protein Kinase | Zendy

John B. Shabb | Zendy; Daryl K. Granner | Zendy

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Separation of Topoisomerase I Activity from the Regulatory Subunit of Type II CyclicAdenosine Monophosphate-Dependent Protein Kinase

Author(s) -

John B. Shabb,

Daryl K. Granner

Publication year - 1988

Publication title -

molecular endocrinology

Language(s) - English

Resource type - Journals

eISSN - 1944-9917

pISSN - 0888-8809

DOI - 10.1210/mend-2-4-324

Subject(s) - topoisomerase , biology , protein subunit , protein kinase a , biochemistry , affinity chromatography , kinase , microbiology and biotechnology , enzyme , gene

The cAMP-containing phosphoform of the regulatory subunit (RII) of type II cAMP-dependent protein kinase from rat liver has been reported to have intrinsic DNA topoisomerase I activity. We found that highly purified RII preparations from eight different sources, including rat liver, contained no detectable topoisomerase I activity. Topoisomerase I exhibited an overlapping peak of activity with RII when rat liver extracts were fractionated by diethylaminoethyl-cellulose chromatography. Topoisomerase I activity was separated from RII by subsequent cAMP affinity chromatography. The results indicate that the regulatory subunit of cAMP-dependent protein kinase does not contain intrinsic topoisomerase I activity.

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