The phosphotransferase system of human central-nervous-system myelin was investigated. Evidence obtained indicated the presence of at least two different phosphotransferase systems (cyclic nucleotide-dependent and -independent) in myelin, which were found to be firmly associated with the membrane. The cyclic AMP-dependent kinase of myelin and white-matter cytosol preferentially phosphorylated certain histone fractions and displayed only modest activity with basic protein as substrate. On the other hand, the cyclic nucleotide-independent system showed specificity toward basic protein. Its activity was not only dependent on Mg2+ but it was greatly enhanced by this bivalent cation. Whereas the cyclic nucleotide-dependent kinase could be extracted with buffers containing Triton X-100, the bivalent cation-regulated kinase resisted solubilization from myelin under these conditions.
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Research Article| March 01 1983
Partial characterization of the phosphotransferase system of human central-nervous-system myelin
Biochem J (1983) 209 (3): 789–795.
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N C Wu, J E Yourist, W D Rector, F Ahmad; Partial characterization of the phosphotransferase system of human central-nervous-system myelin. Biochem J 1 March 1983; 209 (3): 789–795. doi: https://doi.org/10.1042/bj2090789
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