Biochemical and Biophysical Research Communications 1990-02-14

A synthetic peptide substrate for selective assay of protein kinase C.

I Yasuda, A Kishimoto, S Tanaka, M Tominaga, A Sakurai, Y Nishizuka

Index: Biochem. Biophys. Res. Commun. 166 , 1220, (1990)

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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.