Two components of type III protein kinase C with different substrate specificities and a phospholipid-dependent but Ca2+-inhibited protein kinase in rat brain

Lázló Buday, György Mészáros, Gyöngyi Farkas, János Seprodi, Ferenc Antoni, Anna Faragó

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Abstract

The activities of rat brain protein kinase C isoenzymic fractions separated by hydroxyapatite chromatography were measured with histone H1 or the oligopeptide Ala-Ala-Ala-Ser-Phe-Lys-Ala-Lys-Lys-amide as substrates. The oligopeptide was a better substrate than histone H1 for nearly all of the protein kinase C fractions. Two subtractions of type III isoenzyme were resolved (IIIa and IIIb); type IIIb was characterized by a very low histone kinase activity compared to its peptide kinase activity. In some brain extracts a phospholipid-dependent but Ca2+-inhibited protein kinase was also observed which was eluted from the hydroxyapatite column between type II and III isoenzymes of protein kinase C.

Original languageEnglish
Pages (from-to)324-328
Number of pages5
JournalFEBS letters
Volume249
Issue number2
DOIs
Publication statusPublished - Jun 5 1989

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Keywords

  • Ca-inhibited enzyme
  • Isoenzyme
  • Protein kinase C
  • Substrate specificity
  • Synthetic oligopeptide substrate

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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