Specific substrate for histone kinase II

a synthetic nonapeptide

Tibor Romhányi, J. Seprődi, Ferenc Antoni, György Mészáros, A. Faragó

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

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
Volume827
Issue number2
DOIs
Publication statusPublished - Feb 4 1985

Fingerprint

Protamine Kinase
Phosphorylation
Histones
Peptides
Substrates
Complex Mixtures
Thymus
Enzymes
Substrate Specificity
Amides
Liver
Thymus Gland
Spleen
Tissue

Keywords

  • Histone kinase
  • Protein phosphorylation
  • Synthetic peptide

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Structural Biology

Cite this

Specific substrate for histone kinase II : a synthetic nonapeptide. / Romhányi, Tibor; Seprődi, J.; Antoni, Ferenc; Mészáros, György; Faragó, A.

In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 827, No. 2, 04.02.1985, p. 144-149.

Research output: Contribution to journalArticle

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