A synthetic peptide substrate for selective assay of protein kinase C

  • Biochem Biophys Res Commun. 1990 Feb 14;166(3):1220-7. doi: 10.1016/0006-291x(90)90996-z.
I Yasuda  1 ,  A Kishimoto ,  S Tanaka ,  M Tominaga ,  A Sakurai ,  Y Nishizuka
Affiliations
  • 1. Department of Biochemistry, Kobe University School of Medicine, Japan.
PMID: 1689574 DOI: 10.1016/0006-291x(90)90996-z
Abstract

Among various phosphate acceptor proteins and peptides so far tested, a synthetic peptide having the sequence surrounding Ser(8) of myelin basic protein, Gln-Lys-Arg-Pro-Ser(8)-Gln-Arg-Ser-Lys-Tyr-Leu, (MBP4-14), is the most specific and convenient substrate which can be used for selective assay of protein kinase C. This peptide is not phosphorylated by cyclic AMP-dependent protein kinase, casein kinases I and II, Ca2+/calmodulin-dependent protein kinase II, or Phosphorylase kinase, and can be routinely used for the assay of protein kinase C with low background in the crude tissue extracts. The Km value is considerably low (7 microM) with a Vmax value of twice as much as that for H1 histone.

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