http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
Ontogeny of the cyclic amp-dependent protein kinase in the developing chick brain
Ontogenic relationships between levels of cAMP binding activity and protein kinase activity were examined in subcellular fractions of the brain from day 10 of embryogenesis to day 14 post hatch. The cytoplasmic fraction showed no embryonic changes in protein kinase activity, but did increase rapidly from hatch to day 3 post hatch. Both the nuclear and particulate fractions showed a progressive increase in activity during embryogenesis that continued till day 3 post hatch for the particulate fraction and day 14 post hatch for the nuclei. Use of the heat stable protein kinase inhibitor showed that the protein kinase activity of the cytoplasmic and particulate fractions were predominately cAMP-dependent with that of the nuclei being predominately cAMP-independent. The changes in cAMP binding do not parallel that of the protein kinase activity and show no change in activity throughout development. Characterization of the protein kinase isoenzymes by DEAE-cellulose chromatography reveals a type I and II isoenzyme in the cytoplasm and that the post natal changes are due to an increase in type I isoenzyme. The isoenzyme pattern of the particulate fraction shows it to be predominately type II.
Ph. D. in Philosophy Texas A & M University 1982
Includes bibliographical references (leaves 111-116).