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Two Developmentally Regulated Isoenzymes of Calmodulin‐Stimulated Protein Kinase II in Rat Forebrain
Author(s) -
Rostas John A. P.,
Seccombe Margaret,
Weinberger Ron P.
Publication year - 1988
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1988.tb03003.x
Subject(s) - forebrain , isozyme , protein subunit , calmodulin , enzyme , molecular mass , biochemistry , biology , protein kinase a , kinase , microbiology and biotechnology , silver stain , endocrinology , gene , central nervous system
Soluble calmodulin‐stimulated protein kinase II has been purified from adult and 10‐day‐old rat forebrain. By autoradiography, the α/β subunit ratios of the 10‐day and adult enzymes were 0.67 ± 0.03 and 2.20 ±0.15, respectively. By silver staining, the α/β 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.