Intrinsic Protein Phosphorylation in Synaptosomal Plasma Membrane Fragments: A Comparison of Cerebral Cortex Tissue from Several Species, Including Human Biopsy Specimens |
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Authors: | Luis Martinez-Millan Richard Rodnight |
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Institution: | Department of Biochemistry, Institute of Psychiatry, De Crespigny Park, London, U.K. |
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Abstract: | 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 Ca2+-dependent protein kinase activity. Ox brain obtained from a slaughterhouse yielded membranes containing no Ca2+-dependent protein kinase activity, but this may have been due to unavoidable postmortem losses. |
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Keywords: | Protein phosphorylation Cyclic AMP Calciumions Calmodulin Species variation Human biopsy brain tissue |
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