Phosphorylation of 68 kDa neurofilament proteins has no significant effect on their assembly

• Authors: A. Sonska , G. Entlicher
• Languages of publication: EN

Abstracts

EN

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.

Keywords

EN

ELECTRON MICROSCOPE; NEUROFILAMENTS; PHOSPHORYLATION

Discipline

• EXPERIMENTAL_BIOLOGY_&_MEDICINE: EXPERIMENTAL BIOLOGY & MEDICINE

• Publisher: Marceli Nencki Institute of Experimental Biology, Polish Academy of Sciences
• Journal: Acta Neurobiologiae Experimentalis
• Year: 1997
• Volume: 57
• Issue: 4
• Pages: 333-338

Contributors

author

A. Sonska

author

G. Entlicher

• Document Type: article
• Publication order reference: A.Sonska, Department of Biochemistry, Charles University, 2030 Albertov St.,128 43 Prague 2, Czech Republic