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A novel Ca2+/calmodulin-dependent protein kinase lacking autophosphorylation activity in the rabbit heart.

Abstract：

:We report the discovery, semi-purification and characterization of a novel Ca2+/calmodulin-dependent protein kinase (peak I kinase) using syntide 2 as a substrate from the rabbit heart. In the study of dependence of peak I kinase on the concentration of calmodulin, half-maximal activation was obtained at approx. 2.0 x 10(-7) M calmodulin. Peak I kinase did not undergo autophosphorylation. This kinase phosphorylates the synthetic peptides such as syntide 2, autocamtide-2, site 3 in a Ca2+/CaM-dependent manner, but not myosin light chain-peptide, gamma-peptide, and cAMP Response Element Binding Protein (CREB) peptide. Elongation Factor-2, alpha-casein and histone-IIIs were not phosphorylated. These data indicate that this CaM kinase is different from other identified Ca2+/calmodulin-dependent protein kinases and therefore constitutes a novel protein kinase.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Uemura A,Okazaki K,Takesue H,Matsubara T,Hidaka H

doi

10.1006/bbrc.1995.1850

subject

Has Abstract

pub_date

1995-06-15 00:00:00

pages

562-9

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(85)71850-5

journal_volume

211

pub_type

杂志文章

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