Abstract
CEREBRAL membrane fragments contain intrinsic kinase systems transferring the γ-phosphate of ATP to protein bound serine residues in the membrane structure1. The acceptor molecules may be enzymes the activities of which are modified by phosphorylation or non-enzymic phosphoproteins of the classical type represented by casein and phosvitin2. There is indirect evidence for the latter interpretation, for membrane preparations exhibit kinase activity towards casein and phosvitin3, and a soluble protein kinase which also transfers to these proteins has been extracted from microsomes4. No example is yet known of the phosphorylation of a membrane-bound enzyme by a membrane-bound kinase. In the cell cytoplasm, on the other hand, phosphorylation of glycogen phosphorylase has been extensively studied and apparently involves two distinct protein kinases5. One of these kinases, tentatively named phosphorylase kinase kinase, is stimulated by cyclic 3′5′-adenosine monophosphate (cyclic AMP)6. This article reports a similar effect of cyclic AMP on a membrane-bound protein kinase system.
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WELLER, M., RODNIGHT, R. Stimulation by Cyclic AMP of Intrinsic Protein Kinase Activity in Ox Brain Membrane Preparations. Nature 225, 187–188 (1970). https://doi.org/10.1038/225187a0
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DOI: https://doi.org/10.1038/225187a0
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