Abstract

ADP-ribosylation of neurofilaments by an ADP-ribose transferase isolated from cytoplasmic ribonucleoprotein particles is demonstrated. The 150 kDa neurofilament subunit appears to be the main ADP-ribose acceptor with the transfer of ADP-ribose dimers or monomers. A binding of about 1 mole ADP-ribose per 8 moles of neurofilament subunits has been recorded. An interaction between neurofilaments′ ADP-ribosylation and their phosphorylation state is demonstrated.

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