Purification and Characterization of Active Fragment of Ca2+/Calmodulin-Dependent Protein Kinase II from the Post-Synaptic Density in the Rat Forebrain.

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概要

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• 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 α-chymotrypsin digestion with prior autophosphorylation of the kinase. The enzyme was also activated by trypsin and μ-calpain, a Ca2+-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.

• 社団法人 日本生化学会の論文

著者

• Nomura Tomohiko

  Department Of Biochemistry Faculty Of Pharmaceutical Sciences Tokushima Bunri University

• Yoshimura Yoshiyuki

  Department Of Biochemistry Faculty Of Pharmaceutical Sciences The University Of Tokushima

• Yamauchi Takashi

  Department Of Applied Physics Faculty Of Engineering Osaka University

• YAMAUCHI Takashi

  Department of Biochemistry, Faculty of Pharmaceutical Sciences, The University of Tokushima

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