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Intrinsic Protein Phosphorylation in Synaptosomal Plasma Membrane Fragments: A Comparison of Cerebral Cortex Tissue from Several Species, Including Human Biopsy Specimens
Author(s) -
MartinezMillan Luis,
Rodnight Richard
Publication year - 1982
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.1471-4159.1982.tb12570.x
Subject(s) - phosphorylation , membrane , protein kinase a , cerebral cortex , biochemistry , kinase , synaptosome , biology , protein phosphorylation , guinea pig , chemistry , biophysics , microbiology and biotechnology , endocrinology
Intrinsic protein phosphorylation was studied in synaptosomal membrane fragments made from cerebral cortex tissue taken from the following species: human (biopsy specimens), ox, rat, rabbit, guinea pig and mouse. Membrane fragments from all species exhibited a qualitatively similar range of protein acceptors phosphorylated by cyclic AMP‐dependent protein kinase activity; contrary to a previous report, no evidence for cyclic GMP‐dependent protein kinase activity was found in the human material. With the exception of membrane fragments prepared from ox brain, all the preparations exhibited the same range of Ca 2+ ‐dependent protein kinase activity. Ox brain obtained from a slaughterhouse yielded membranes containing no Ca 2+ ‐dependent protein kinase activity, but this may have been due to unavoidable postmortem losses.