A modified paper-binding procedure for the assay of nucleus-associated protein phosphokinases

Said A. Goueli, Rolv Slungaard, Michael J Wilson, Khalil Ahmed

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

Previously existing paper-binding assay procedures gave results with large variations when employed for the measurement of nucleus-associated protein phosphokinase activities. However, a modified method, utilizing the binding of 32Plabeled phosphoprotein substrates to paper and employing washing procedures in 20% trichloroacetic acid at 60° to 70°C, gave highly reproducible results. This modified procedure was satisfactory with either chromatin or a nonhistone protein fraction derived therefrom as a source of enzyme, and dephosphophosvitin, lysine-rich histones, or casein as phosphoprotein substrates.

Original languageEnglish (US)
Pages (from-to)235-242
Number of pages8
JournalJournal of Pharmacological Methods
Volume3
Issue number3
DOIs
StatePublished - May 1980

Keywords

  • Casein
  • Chromatin
  • Dephosphophosvitin
  • Lysine-rich histones
  • Nonhistone proteins
  • Nucleus
  • Protein Phosphokinases
  • Protein kinase assay

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