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Effects of Hydrazines and Related Compounds on Calcium-Calmodulin Regulated Neuronal Processes.
Final rept. 1 Jul 85-1 Feb 87,
MEDICAL COLL OF VIRGINIA RICHMOND DEPT OF NEUROLOGY
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Results from this investigation have provided a basic understanding of how calcium regulates neuronal cytoskeletal function. Calmodulin-dependent protein kinase activity was investigated in cold stable and cold labile microtubule fractions. Calmodulin-dependent kinase was enriched approximately twenty fold over Cytosol in cold stable microtubule preparations. Calmodulin-dependent Kinase activity in cold stable microtubule preparations phosphorylated microtubule associated protein-2, tubulin, an 80,000 dalton doublet, and several minor phosphoproteins. This endogenous calmodulin-dependent kinase in cold stable microtubule fractions was identical to CaM-Kinase II isolated from rat brain by several criteria including 1 subunit molecular weights, 2 subunit isoelectric points, 3 calmodulin binding properties, 4 subunit autophophorylation, 5 Calmodulin binding subunit composition, 6isolation of kinase on calmodulin affinity resin, 7 kinetic parameters, 8 phosphoamino acid phosphorylation sites on tubulin, and, 9 phosphopeptide mapping. Endogenous cold stable calmodulin-dependent kinase activity was isolated from the microtubule fraction by calmodulin affinity resin column chromatography and specifically eluded with EGTA. This kinase fraction contained the calmodulin binding protein and autophosphorylating subunits of CaM Kinase II.
APPROVED FOR PUBLIC RELEASE