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Native low molecular weight neurofilaments (NF L) from bovine spinal cord with original phosphate content of 0.4 moles of phosphate per 1 mol of protein were phosphorylated with cyclic AMP dependent protein kinase and protein kinase C. In a similar way recombinant mouse NF L proteins which did not contain any phosphate were phosphorylated with the same enzymes in both, the assembled and disassembled forms. The final phosphate content in both types of NF L proteins reached about 4 moles of phosphate per 1 mol of protein. This phosphorylation had no effect on the assembly of NF L into filaments as observed by electron microscopy.
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333-338
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A.Sonska, Department of Biochemistry, Charles University, 2030 Albertov St.,128 43 Prague 2, Czech Republic
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bwmeta1.element.element-from-psjc-f9d4d4ff-fd49-363a-bc7f-29367847004e