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- W1634621704 abstract "The selective binding of protein kinase C to nitrocellulose-immobilized polypeptides from rat brain and human erythrocytes was investigated. Bound enzyme was detected immunochemically with a monospecific protein kinase C antibody, or by using radiolabeled enzyme. Two polypeptides from erythrocyte membranes with Mr values of 110,000 and 115,000 bound protein kinase C in the presence of phosphatidylserine (PS) and were highly enriched in the cytoskeletal fraction. A prominent protein kinase C-binding polypeptide at Mr about 115,000 was also evident in brain cytoplasm, postsynaptic densities, and nuclei. Overlays of electrophoretic blots with 14C-phospholipids revealed that the protein kinase C-binding polypeptides also bound PS but not other phospholipids. The binding of both protein kinase C and PS was markedly inhibited after phosphorylation of the Mr 110,000/115,000 polypeptides with the kinase itself. The relevance of the results to the binding of protein kinase C to membranes and to phospholipid-cytoskeletal interactions is discussed." @default.
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- W1634621704 date "1986-10-01" @default.
- W1634621704 modified "2023-09-30" @default.
- W1634621704 title "Protein kinase C and phosphatidylserine bind to Mr 110,000/115,000 polypeptides enriched in cytoskeletal and postsynaptic density preparations." @default.
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- W1634621704 doi "https://doi.org/10.1016/s0021-9258(18)69308-1" @default.
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