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  • Title: Purification and characterization of active fragment of Ca2+/calmodulin-dependent protein kinase II from the post-synaptic density in the rat forebrain.
    Author: Yoshimura Y, Nomura T, Yamauchi T.
    Journal: J Biochem; 1996 Feb; 119(2):268-73. PubMed ID: 8882717.
    Abstract:
    Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) of the post-synaptic density (PSD) was solubilized and activated 4- to 5-fold by limited alpha-chymotrypsin digestion with prior autophosphorylation of the kinase. The enzyme was also activated by trypsin and mu-calpain, a Ca(2+)-dependent protease. The active catalytic fragment was purified to homogeneity using gel filtration and ion exchange chromatography. The purified active fragment was completely Ca2+/calmodulin-independent and exists as a monomer. Kinetic studies with the purified fragment revealed similar Km values for ATP and synthetic peptide substrate, and an about 8-fold increment in Vmax, compared with native PSD CaM kinase II.
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