Studies on a cyclic nucleotide-independent protein kinase and its proenzyme in mammalian tissues. II. Proenzyme and its activation by calcium-dependent protease from rat brain.
Journal of Biological ChemistryPublished 1 November 1977Open access
Masatoshi Inoue, Akira Kishimoto, Yoshimi Takai, Yasutomi Nishizuka
Citations864
SJR quartileQ1
SJR score1.71
SNIP1.00
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TL;DR
A protein kinase which phosphorylated histone and protamine was partially purified from bovine cerebellum and preliminary analysis suggested that the enzyme was produced from its precursor protein by a limited proteolytic reaction.
Abstract
was found in the soluble fraction of rat brain.Upon limited proteolysis by calcium-dependent protease occurring in the same tissue, the proenzyme was converted to an active protein kinase which could phosphorylate five species of histone fractions.Trypsin also catalyzed the conversion.
Keywords
MedicineBiochemistry, Genetics and Molecular BiologyPharmacology, Toxicology and Pharmaceutics
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