IDENTIFICATION, CHARACTERIZATION, IMMUNOCYTOCHEMICAL LOCALIZATION, AND DEVELOPMENTAL-CHANGES IN THE ACTIVITY OF CALCIUM CALMODULIN-DEPENDENT PROTEIN-KINASE-II IN THE CNS OF BOMBYX-MORI DURING POSTEMBRYONIC DEVELOPMENT/

In the present investigation, in vitro phosphorylation of CNS proteins of the silkworm Bombyx mori during the postembryonic development have been studied, Sodium dodecyl sulfate-polyacrylamide gel electrophores is and autoradiography of phosphorylated proteins revealed the presenc e of major phosphoproteins of 59/60 kDa, Based on molecular mass, calc ium/calmodulin-dependent autophosphorylation, substrate specificity, K N-62 inhibition, apparent K-m far ATP and syntide-2, these proteins we re identified as calcium/calmodulin-dependent protein kinase II (CaM k inase II). Anti-rat CaM kinase II monoclonal antibody showed immunorea ctivity with Bombyx CaM kinase II isoforms. This kinase showed a high degree of autophosphorylation in neural tissue, During postembryonic d evelopment of Bombyx, two distinct peaks of enzyme activity could be n oticed, one at the late-larval and another at the late-pupal stage, wh ich were associated with an increase in amount of the enzyme, These re sults suggested that the expression of CaM kinase II in the CNS of Bom byx was developmentally regulated.