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- W2000470332 abstract "Myelin isolated from the rat peripheral nervous system (sciatic nerve and cauda equina) contained Mg 2+ -dependent protein kinase that phosphorylated myelin polypeptides. Ca 2+ , in micromolar concentrations, markedly stimulated phosphorylation (half-maximal stimulation at 5 μM (free) Ca 2+ ) but at higher concentrations (> 100 μM Ca 2+ ) it caused inhibition. In the presence of Triton X-100, phosphorylation (±Ca 2+ ) of myelin was increased and Ca 2+ caused up to a 10-fold increase in phosphorylation. Among the myelin polypeptides, P 0 (M r , 28 000), a major glycoprotein, accounted for nearly 60% of the total phosphate incorporated into the myelin and Ca 2+ markedly promoted phosphorylation of P 0 . Phosphorylation of other myelin polypeptides, P 2 (M r , 16 000), Y (M r , 26 000), and P 1 (M r , 20 000), and the Ca 2+ -stimulatory effect on phosphorylation of these were also evident. Cyclic AMP (or other cyclic nucleotides) failed to show any significant stimulatory effect on myelin phosphorylation." @default.
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- W2000470332 date "1979-10-01" @default.
- W2000470332 modified "2023-09-24" @default.
- W2000470332 title "Calcium ion stimulated endogenous protein kinase catalyzed phosphorylation of peripheral nerve myelin proteins" @default.
- W2000470332 doi "https://doi.org/10.1139/y79-181" @default.
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