Two Developmentally Regulated Isoenzymes of Calmodulin‐Stimulated Protein Kinase II in Rat Forebrain

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Abstract
Soluble calmodulin-stimulated protein kinase II has been purified from adult and 10-day-old rat forebrain. By autoradiography, the .alpha./.beta. subunit ratios of the 10-day and adult enzymes were 0.67 .+-. 0.03 and 2.20 .+-. 0.15, respectively. By silver staining the .alpha./.beta. subunit ratios were 1.02 .+-. 0.06 and 2.36 .+-. 0.10, respectively. The apparent holoenzyme molecular masses of the purified 10-day and adult enzymes were 500,000 daltons and 700,000 daltons. However, varying the purification conditions revealed higher and lower molecular mass forms at both ages and suggested that the form of the kinase that is usually purified is merely that which has the highest affinity for calmodulin-Sepharose and may not be the form of the kinase that exists in vivo. The subunits of the adult and 10-day enzymes were indistinguishable by one- and two-dimensional electrophoresis and one-dimensional proteolytic peptide maps. These results are consistent with the suggestion that at least two developmentally regulated isoenzymes of this kinase exist in rat forebrain.

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