Efficacy of the phosphorylation of synthetic peptides by purified catalytic subunit of PKA (PKAcat) from bovine lens depends on the amino acid sequence of the peptides

B. Samanta, G. Mezö, K. P. Das, A. C. Ghose, F. Hudecz, P. C. Sen

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Protein kinase (PK) A catalytic (PKAcat) subunit was purified to homogeneity from bovine lens using a 100-kDa cut-off membrane filtration followed by different chromatographic procedures. The molecular weight of PKAcat was found to be 41 kDa. The kinase phosphorylates histone IIIs and other synthetic modified peptides of VRKRTLRRL with different amino acid environment. The extent of phosphorylation depends not only on the presence of Ser or Thr (phosphorylating residues) but also on other surrounding amino acid residues. Although some peptides compete in phosphorylating histone, they are not very significant. The result suggests that the extent of phosphorylation depends on the amino acid residue(s) surrounding phosphorylable residue(s) on the peptide. Copyright Blackwell Munksgaard, 2005.

Original languageEnglish
Pages (from-to)445-449
Number of pages5
JournalJournal of Peptide Research
Volume65
Issue number4
DOIs
Publication statusPublished - Apr 1 2005

Keywords

  • Bovine lens
  • Phosphorylation
  • Protein kinase A catalytic subunit
  • Synthetic peptides

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology

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