Specific substrate for histone kinase II: a synthetic nonapeptide

Tibor Romhányi, János Sepródi, Ferenc Antoni, György Mészáros, Anna Faragó

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Based on the previously determined intrinsic substrate specificity of histone kinase II, a nonapeptide was synthesized which was a specific substrate for this enzyme. The Vmax value of phosphorylation of the peptide (Ala-Ala-Ala-Ser-Phe-Lys-Ala-Lys-Lys-amide) was about the same as that for H1 histone and the apparent Km for the phosphorylation of the peptide was 0.2 mM, an order of magnitude higher than that for H1 histone. H1 histone inhibited the phosphorylation of the peptide, while the peptide did not inhibit the phosphorylation of H1 histone. In the crude extracts of calf thymus, spleen and liver, histone kinase II was the only enzyme which phosphorylated the synthetic peptide. The rate of phosphorylation of this peptide was used to determine the activity of histone kinase II in the crude extracts of several tissues obtained from different species.

Original languageEnglish
Pages (from-to)144-149
Number of pages6
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Issue number2
Publication statusPublished - Feb 4 1985



  • Histone kinase
  • Protein phosphorylation
  • Synthetic peptide

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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