A synthetic peptide substrate for selective assay of protein kinase C
I Yasuda, A Kishimoto, S Tanaka, M Tominaga… - Biochemical and …, 1990 - Elsevier
I Yasuda, A Kishimoto, S Tanaka, M Tominaga, A Sakurai, Y Nishizuka
Biochemical and biophysical research communications, 1990•ElsevierAmong 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,(MBP 4–14), 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, Ca 2+/calmodulin-dependent
protein kinase II, or phosphorylase kinase, and can be routinely used for the assay of protein …
having the sequence surrounding Ser (8) of myelin basic protein, Gln-Lys-Arg-Pro-Ser (8)-
Gln-Arg-Ser-Lys-Tyr-Leu,(MBP 4–14), 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, Ca 2+/calmodulin-dependent
protein kinase II, or phosphorylase kinase, and can be routinely used for the assay of protein …
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 μM) with a Vmax value of twice as much as that for Hl histone.
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