Absence of inactivation or phosphorylation of ornithine decarboxylase by nuclear protein kinase NII and of immunological cross-reactivity between RNA polymerase I and ornithine decarboxylase

James E. Seely, Dean A. Stetler, Samson T. Jacob, Anthony E. Pegg

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

Incubation with protein kinase NII did not result in phosphorylation or inactivation of mouse kidney ornithine decarboxylase. Partially purified ornithine decarboxylase preparations contained a protein kinase activity and stimulated the activity of RNA polymerase I. However, these properties were due to contaminating protein(s) since further purification reduced the kinase activity and removal of the ornithine decarboxylase with a specific antiserum did not abolish the ability to stimulate RNA polymerase I. Antibodies to RNA polymerase I did not interact with ornithine decarboxylase and antibodies to ornithine decarboxylase did not interact with RNA polymerase I. These results indicate that: a) mammalian ornithine decarboxylase activity is not regulated by phosphorylation by protein kinase NII or the contaminating kinase, and b) the ability of impure preparation of ornithine decarboxylase to stimulate RNA polymerase I is due to a contaminating unrelated protein.

Original languageEnglish (US)
Pages (from-to)219-225
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume120
Issue number1
DOIs
StatePublished - Apr 16 1984

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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