Cytoskeletal calmodulin-dependent protein kinase. Characterization, solubilization, and purification from rat brain

N. Sahyoun, H. LeVine, D. Bronson, F. Siegel-Greenstein, P. Cuatrecasas

Research output: Contribution to journalArticlepeer-review

73 Scopus citations

Abstract

Brain calmodulin-dependent protein kinase was isolated as the major cytoskeletal component of the postsynaptosomal fraction, accounting for about 50% of the total protein. The α- and β-subunits of the enzyme were present in a ratio of about 6:1. The cytoskeletal preparation was also distinguished by the regular presence of tubulin and actin in approximately equimolar amounts to the β-subunit. Electron microscopic morphology suggested that the enzyme formed a hierarchy of cytoskeletal complexes with an average diameter of 85 nm. These results indicate that cytoskeletal calmodulin-dependent protein kinase may have a structural as well as a catalytic role in neurons. The cytoskeletal enzyme could be solubilized in 8 M urea, displaying similar properties to its cytosolic counterpart. The postsynaptosomal cytoskeleton provides a simplified and well-defined model for the study of the protein-protein interactions involving calmodulin-dependent protein kinase.

Original languageEnglish
Pages (from-to)1230-1237
Number of pages8
JournalJournal of Biological Chemistry
Volume260
Issue number2
StatePublished - 1985

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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